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Bethyl smc2
Smc2, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/a300+058a/SMC2+Antibody/pm40133469-276-230-231
Average 93 stars, based on 39 article reviews

smc2 - by Bioz Stars, 2026-11

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Article Title: Replication stress induces sister-chromatid bridging at fragile site loci in mitosis.
Article Snippet: Several inherited syndromes in humans are associated with cancer predisposition.. The gene products defective in two of these disorders, BLM (a helicase defective in Bloom’s syndrome)1 and FANC A–N (defective in Fanconi anaemia)2, associate in a multienzyme complex called BRAFT3.. How these proteins suppress tumorigenesis remains unclear, although both conditions are associated with chromosome instability.

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A) Scheme with the multiple strategies employed to interfere with mitotic chromosome structure. B) Quantification of the orientation bias in NE fluctuations for control cells (DMSO; n=30) and cells treated with either ICRF-193 (n=29; p<0.0481) or VPA (n=27; p<0.0461). Values above zero reflect a bias towards inwards fluctuations. C) Representative frames from movies of cells expressing cyclin B1-Venus/H2B-RFP treated with DMSO (top panel), ICRF-193 (middle panel) or VPA (bottom panel). Time is represented in minutes (min) and zero corresponds to the moment of CDK1i washout. D) Quantification of the time for cyclin B1 nuclear translocation after CDK1i washout to for the indicated treatments (n=43 for DMSO; n=38 for ICRF-193; n=43 for VPA; p<0.0001). E) Cumulative percentage of cells with cyclin B1 nuclear translocation following CDK1i washout. F) Representative frames of HeLa cells expressing DHC-GFP cells during mitotic entry, after treatment with DMSO (top panel) or ICRF-193 (bottom panel). Yellow arrowheads indicate the NE. Right panels show kymographs highlighting the absence of dynein on the NE of ICRF-193 treated cells. Horizontal scale bar, 10 μm. Vertical scale bar, 200 sec. G) Representative immunofluorescence images of prophase cells expressing DHC-GFP after treatment with DMSO, ICRF-193 or VPA. H) Quantification of the levels of DHC-GFP fluorescence intensity on the NE for DMSO (n=52), ICRF-193 (n=63) or VPA (n=49) treated cells (p<0.0001). I) Representative immunofluorescence images of DHC-GFP localization at the NE, following depletion of SMC2 by RNAi. J) Quantification of the levels of DHC-GFP on the NE following for control cells (n=74) or SMC2-depleted cells (SMC2 RNAi; n= 33; p<0.0001). Scale bars, 10 μm.

Journal: bioRxiv

Article Title: Chromosome condensation mechanically primes the nucleus for mitosis

doi: 10.1101/2025.09.01.673438

Figure Lengend Snippet: A) Scheme with the multiple strategies employed to interfere with mitotic chromosome structure. B) Quantification of the orientation bias in NE fluctuations for control cells (DMSO; n=30) and cells treated with either ICRF-193 (n=29; p<0.0481) or VPA (n=27; p<0.0461). Values above zero reflect a bias towards inwards fluctuations. C) Representative frames from movies of cells expressing cyclin B1-Venus/H2B-RFP treated with DMSO (top panel), ICRF-193 (middle panel) or VPA (bottom panel). Time is represented in minutes (min) and zero corresponds to the moment of CDK1i washout. D) Quantification of the time for cyclin B1 nuclear translocation after CDK1i washout to for the indicated treatments (n=43 for DMSO; n=38 for ICRF-193; n=43 for VPA; p<0.0001). E) Cumulative percentage of cells with cyclin B1 nuclear translocation following CDK1i washout. F) Representative frames of HeLa cells expressing DHC-GFP cells during mitotic entry, after treatment with DMSO (top panel) or ICRF-193 (bottom panel). Yellow arrowheads indicate the NE. Right panels show kymographs highlighting the absence of dynein on the NE of ICRF-193 treated cells. Horizontal scale bar, 10 μm. Vertical scale bar, 200 sec. G) Representative immunofluorescence images of prophase cells expressing DHC-GFP after treatment with DMSO, ICRF-193 or VPA. H) Quantification of the levels of DHC-GFP fluorescence intensity on the NE for DMSO (n=52), ICRF-193 (n=63) or VPA (n=49) treated cells (p<0.0001). I) Representative immunofluorescence images of DHC-GFP localization at the NE, following depletion of SMC2 by RNAi. J) Quantification of the levels of DHC-GFP on the NE following for control cells (n=74) or SMC2-depleted cells (SMC2 RNAi; n= 33; p<0.0001). Scale bars, 10 μm.

Article Snippet: The following primary antibodies were used: mouse anti-Lamin A/C (1:500, Abcam), rabbit anti-Lamin B1 (1:500, Abcam), rat anti-alpha tubulin (1:500, Bio-Rad), rabbit anti-NudE/NudEL antibody (1:500, gift from Richard Vallee), rabbit anti-BicD2 (1:500, Atlas Antibodies) rabbit anti-SUN1 (1:1000, Sigma-Aldrich), rabbit anti-SUN2 (1:1000, Sigma-Aldrich), rabbit anti-SMC2 antibody (1:500; Bethyl Laboratories) rabbit anti-cPLA2 (1:100, #2832; Cell Signaling), rabbit anti-CENP-F (ab5, 1:300; Abcam).

Techniques: Control, Expressing, Translocation Assay, Immunofluorescence, Fluorescence

A) Representative immunofluorescence images of the NE of prophase cells following disruption of chromosome structure. B) Quantification of the excess of perimeter (EOP) in nuclei of interphase (n=59) and prophase (n=56) cells treated with DMSO, as well as prophase cells treated with ICRF-193 (n=56) or VPA (n=49; p<0.0001). C) Representative immunofluorescence images of nuclei stained for cPLA2 in control cells (DMSO, n=53), and cells treated with ICRF-193 (n=52) or VPA (n=46) in prophase. D) Quantification of cPLA2 levels in the NE and nucleus of DMSO, ICRF-193 (p<0.0001) or VPA (p<0.0001) treated prophase cells. E) Representative immunofluorescence images of nuclei stained for cPLA2 in control (scramble RNAi; n=37) or SMC2 depleted cells (SMC2 RNAi; n=39). F) Quantification of the EOP in nuclei of prophase cells treated with control or SMC2 RNAi (p<0.0001). G) Quantification cPLA2 in the NE (p<0.0001) and nucleus (p=0.0028) of cells depleted of SMC2 by RNAi. H) Representative TEM images of the NE of cells treated with ICRF-193 in interphase (left panel) and prophase (right panel), highlighting the NE in blue and NPCs in yellow. Quantification of the nuclear pore size (I) and perinuclear space (J) in interphase (n= 6 cells; 67 NPCs) and prophase cells treated with ICRF-193 (n=17 cells; 168 NPCs). Scale bars in immunofluorescence images, 10 μm. Scale bars in TEM images, 100 nm.

Journal: bioRxiv

Article Title: Chromosome condensation mechanically primes the nucleus for mitosis

doi: 10.1101/2025.09.01.673438

Figure Lengend Snippet: A) Representative immunofluorescence images of the NE of prophase cells following disruption of chromosome structure. B) Quantification of the excess of perimeter (EOP) in nuclei of interphase (n=59) and prophase (n=56) cells treated with DMSO, as well as prophase cells treated with ICRF-193 (n=56) or VPA (n=49; p<0.0001). C) Representative immunofluorescence images of nuclei stained for cPLA2 in control cells (DMSO, n=53), and cells treated with ICRF-193 (n=52) or VPA (n=46) in prophase. D) Quantification of cPLA2 levels in the NE and nucleus of DMSO, ICRF-193 (p<0.0001) or VPA (p<0.0001) treated prophase cells. E) Representative immunofluorescence images of nuclei stained for cPLA2 in control (scramble RNAi; n=37) or SMC2 depleted cells (SMC2 RNAi; n=39). F) Quantification of the EOP in nuclei of prophase cells treated with control or SMC2 RNAi (p<0.0001). G) Quantification cPLA2 in the NE (p<0.0001) and nucleus (p=0.0028) of cells depleted of SMC2 by RNAi. H) Representative TEM images of the NE of cells treated with ICRF-193 in interphase (left panel) and prophase (right panel), highlighting the NE in blue and NPCs in yellow. Quantification of the nuclear pore size (I) and perinuclear space (J) in interphase (n= 6 cells; 67 NPCs) and prophase cells treated with ICRF-193 (n=17 cells; 168 NPCs). Scale bars in immunofluorescence images, 10 μm. Scale bars in TEM images, 100 nm.

Techniques: Immunofluorescence, Disruption, Staining, Control, Pore Size

A) Schematic representation of the experimental setup designed to assess the response of the prophase nucleus to mechanical stimulation. B) Representative images of control HeLa cell in prophase expressing DHC-GFP and stained with SiR-DNA under mechanical stimulation. Time zero corresponds to the moment when compression was applied to the nucleus. C) Ratio between the intensity of dynein on the NE and cytoplasm for control prophase cells (n=12). Note how the ratio is above 1, reflecting an enrichment of dynein on the NE during this stage of the cell cycle. D) Representative images of a prophase cell treated with ICRF-193 expressing DHC-GFP and stained with SiR-DNA, under mechanical stimulation. Time zero corresponds to the moment when compression was applied to the nucleus. E) Ratio between the intensity of dynein on the NE and cytoplasm for prophase cells treated with ICRF-193 (n=12). Note how the ratio increases following mechanical stimulation. F) Representative immunofluorescence images of DMSO (n=48), ICRF-193 (n=58) or VPA (n=22) treated cells after confinement, showing localization dynein on the NE. G) Quantification of DHC-GFP levels on the NE after mechanical stimulation. Note how ICRF-193 and VPA-treated cells accumulate dynein on the NE, similar to controls. H) Representative immunofluorescence images of controls (Scramble RNAi) and SMC2 depleted cells (SMC2 RNAi) showing dynein localization on the NE. I) Quantification of DHC-GFP levels on the NE of control cells (n=28) and cells depleted of SMC2 (n=23) after mechanical stimulation. Scale bars, 10 μm.

Journal: bioRxiv

Article Title: Chromosome condensation mechanically primes the nucleus for mitosis

doi: 10.1101/2025.09.01.673438

Figure Lengend Snippet: A) Schematic representation of the experimental setup designed to assess the response of the prophase nucleus to mechanical stimulation. B) Representative images of control HeLa cell in prophase expressing DHC-GFP and stained with SiR-DNA under mechanical stimulation. Time zero corresponds to the moment when compression was applied to the nucleus. C) Ratio between the intensity of dynein on the NE and cytoplasm for control prophase cells (n=12). Note how the ratio is above 1, reflecting an enrichment of dynein on the NE during this stage of the cell cycle. D) Representative images of a prophase cell treated with ICRF-193 expressing DHC-GFP and stained with SiR-DNA, under mechanical stimulation. Time zero corresponds to the moment when compression was applied to the nucleus. E) Ratio between the intensity of dynein on the NE and cytoplasm for prophase cells treated with ICRF-193 (n=12). Note how the ratio increases following mechanical stimulation. F) Representative immunofluorescence images of DMSO (n=48), ICRF-193 (n=58) or VPA (n=22) treated cells after confinement, showing localization dynein on the NE. G) Quantification of DHC-GFP levels on the NE after mechanical stimulation. Note how ICRF-193 and VPA-treated cells accumulate dynein on the NE, similar to controls. H) Representative immunofluorescence images of controls (Scramble RNAi) and SMC2 depleted cells (SMC2 RNAi) showing dynein localization on the NE. I) Quantification of DHC-GFP levels on the NE of control cells (n=28) and cells depleted of SMC2 (n=23) after mechanical stimulation. Scale bars, 10 μm.

Techniques: Control, Expressing, Staining, Immunofluorescence

a SMC2 was identified by mass spectrometry in a co-immunoprecipitate of endogenous BLM from nuclear extracts of WT cells 3 h after release from G1/S arrest . Select known BLM interacting proteins are shown for comparison. Isogenic BLM-KO cells were subjected to the same analysis and yielded zero hits for the listed proteins. Experiment was performed in triplicate. b Reciprocal co-immunoprecipitation of endogenous BLM and SMC2 from nuclear extracts of WT and BLM-KO cells 3 h after release from G1/S arrest. c , Proximity ligation assay (PLA) using antibodies against endogenous BLM and SMC2 in WT, BLM-COMP, and BLM-KO cells 3 h after release from G1/S arrest and quantification of BLM-SMC2 PLA foci/nucleus (WT, n = 111 nuclei; BLM-COMP, n = 103 nuclei; BLM-KO, n = 104 nuclei). Scale bars, 10 μM. Significance of difference between WT and BLM-COMP was determined by a Mann–Whitney test (ns, not significant). For additional PLA controls, see Supplementary Fig. S . d Five-subunit condensin I and II complexes (H, NCAPH; D2, NCAPD2; G, NCAPG; H2, NCAPH2; D3, NCAPD3; G2, NCAPG2). e Co-immunoprecipitation of endogenous BLM from whole-cell extracts of WT cells 3 h after release from G1/S arrest was probed with antibodies against condensin I and II subunits. Condensin subunits are color-coordinated with their respective condensin from ( d ). f Co-immunoprecipitation of endogenous NCAPH from whole-cell extracts of WT cells 3 h after release from G1/S arrest was probed with antibodies against condensin I and II subunits and BLM. g Co-immunoprecipitation of endogenous NCAPH2 from whole-cell extracts of WT cells 3 h after release from G1/S arrest was probed with antibodies against condensin I and II subunits and BLM.

Journal: Communications Biology

Article Title: Condensin II interacts with BLM helicase in S phase to maintain genome stability

doi: 10.1038/s42003-025-07916-0

Figure Lengend Snippet: a SMC2 was identified by mass spectrometry in a co-immunoprecipitate of endogenous BLM from nuclear extracts of WT cells 3 h after release from G1/S arrest . Select known BLM interacting proteins are shown for comparison. Isogenic BLM-KO cells were subjected to the same analysis and yielded zero hits for the listed proteins. Experiment was performed in triplicate. b Reciprocal co-immunoprecipitation of endogenous BLM and SMC2 from nuclear extracts of WT and BLM-KO cells 3 h after release from G1/S arrest. c , Proximity ligation assay (PLA) using antibodies against endogenous BLM and SMC2 in WT, BLM-COMP, and BLM-KO cells 3 h after release from G1/S arrest and quantification of BLM-SMC2 PLA foci/nucleus (WT, n = 111 nuclei; BLM-COMP, n = 103 nuclei; BLM-KO, n = 104 nuclei). Scale bars, 10 μM. Significance of difference between WT and BLM-COMP was determined by a Mann–Whitney test (ns, not significant). For additional PLA controls, see Supplementary Fig. S . d Five-subunit condensin I and II complexes (H, NCAPH; D2, NCAPD2; G, NCAPG; H2, NCAPH2; D3, NCAPD3; G2, NCAPG2). e Co-immunoprecipitation of endogenous BLM from whole-cell extracts of WT cells 3 h after release from G1/S arrest was probed with antibodies against condensin I and II subunits. Condensin subunits are color-coordinated with their respective condensin from ( d ). f Co-immunoprecipitation of endogenous NCAPH from whole-cell extracts of WT cells 3 h after release from G1/S arrest was probed with antibodies against condensin I and II subunits and BLM. g Co-immunoprecipitation of endogenous NCAPH2 from whole-cell extracts of WT cells 3 h after release from G1/S arrest was probed with antibodies against condensin I and II subunits and BLM.

Article Snippet: Commercially available antibodies against the following proteins are as follows with the application and concentration used: β-actin (Santa Cruz, cat. no. sc-69879, WB, 1:5000), Biotin (Jackson Labs, cat. no. 200-002-211, Immunofluorescence (IF), 1:1000; Bethyl, cat. no. A150-109A, IF, 1:1000), BLM (Santa Cruz, cat. no. sc-365753, WB and IF, 1:200 and 1:250; Bethyl, cat. no. A300-110A, IP, 5 μg/mL; Abcam, cat no. ab2179, IF, 1:2000), BrdU (BD Biosciences, cat. no. 347580, IF, 1:50; Abcam, cat. no. ab6326, IF, 1:100), CREST (Antibodies Inc., cat. no. 15-234-0001, IF, 1:50), Cyclin A (Santa Cruz cat. no. sc-239, WB, 1:500), Cyclin B1 (Santa Cruz cat. no. sc-245, WB, 1:1000), Cyclin E (Santa Cruz cat. no. sc-377100, WB, 1:500), GAL4-TA (Santa Cruz, cat. no. sc-1663, WB, 1:200), γ-H2AX (Abcam, cat. no. ab81299, WB, 1:5000), Histone H2A (Invitrogen, cat. no. MA5-24662, WB, 1:1000), Histone H4 (Santa Cruz, cat. no. sc-25260, WB, 1:200), MCM6 (Santa Cruz, cat. no. sc-393618, WB, 1:200), NCAPD3 (Santa Cruz, cat. no. sc-81597, WB, 1:200), NCAPG (Santa Cruz, cat. no. sc-515297, WB, 1:200), NCAPH (Santa Cruz, cat. no. sc-101013, WB, 1:500; Bethyl cat. no. A300-603A, IP, 5 μg/mL), NCAPH2 (Santa Cruz, cat. no. sc-393333, WB and IF, 1:500 and 1:250; Bethyl cat. no. A302-275A, IP, 5 μg/mL), PCNA (Cell Signaling, cat. no. 2586, WB, 1:5000), p-DRP1 (Cell Signaling, cat. no. 4494S, WB, 1:500), p-Histone H3 (Cell Signaling, cat. no. 9701S, WB, 1:500), RAD51 (Santa Cruz, cat. no. sc-398587, WB, 1:200), RPA2 (Santa Cruz, cat. no. sc-56770, WB, 1:200), SMC2 (Bethyl, cat. no. A300-058A, IF and Immunoprecipitation (IP), 1:1000 and 5 μg/mL; Invitrogen, cat. no. GT4312, WB, 1:1000; Cell Signaling, cat. no. 5329, IP, 5 μg/mL; Abcam, cat. no. ab10412, IF, 1:250) SMC4 (Bethyl, cat. no. A300-063A, WB, 1:1000), TOP2A (Santa Cruz, cat. no. sc-365916, WB, 1:200), TOP3A (Abcam, cat. no. ab108493, WB, 1:1000).

Techniques: Mass Spectrometry, Comparison, Immunoprecipitation, Proximity Ligation Assay, MANN-WHITNEY

a BLM truncations tested in mammalian-two-hybrid (M2H) assay against full-length SMC2. Interaction is indicated by secreted alkaline phosphatase (SEAP) activity as ++ (strong), + (mild), and - (absent). See Supplementary Fig. S for measurements of SEAP activity from three experiments. Red box indicates BLM region required for interaction with SMC2. b Alignment of BLM residues 150-184 with BLM from other vertebrates. Residues W154, M157, and F160 were mutated to lysine, referred to as BLM-WMF mut . c SEAP activity detected in M2H assay between two independently generated pVP16-BLM-WMF mut clones (#1, #2) and pM-SMC2. pM3-VP16 is a positive control from the manufacturer expressing a fusion of the GAL4 DNA-binding domain to the VP16 activation domain. Significance of differences between means ± SD was determined by a t -test and is reported as **** p ≤ 0.0001. d Plasmid expressing BLM-WMF mut was stably transfected into BLM-KO cells. Western blot of nuclear extracts from two independently generated BLM-WMF mut clones (#1, #2) and of WT, BLM-KO, and BLM-COMP cells was probed with BLM antibody. PCNA was used as a loading control. Expression levels were analyzed 3 h after release from G1/S arrest. e Co-immunoprecipitations of BLM and BLM-WMF mut #1 were probed with antibodies against SMC2, condensin II-specific subunit NCAPH2, and known BLM-interacting proteins. Whole-cell extracts were prepared from cells 3 h after release from G1/S arrest. f PLA using antibodies against endogenous BLM and NCAPH2 in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells 3 h after release from G1/S arrest. Scale bars, 10 μm. BLM-NCAPH2 PLA foci/nucleus were quantified (BLM-COMP, n = 102 nuclei; BLM-WMF mut #1, n = 130 nuclei; BLM-KO, n = 100 nuclei). Significance of differences was determined by a Mann–Whitney test and is reported as **** p ≤ 0.0001. For additional PLA controls, see Supplementary Fig. S .

Journal: Communications Biology

Article Title: Condensin II interacts with BLM helicase in S phase to maintain genome stability

doi: 10.1038/s42003-025-07916-0

Figure Lengend Snippet: a BLM truncations tested in mammalian-two-hybrid (M2H) assay against full-length SMC2. Interaction is indicated by secreted alkaline phosphatase (SEAP) activity as ++ (strong), + (mild), and - (absent). See Supplementary Fig. S for measurements of SEAP activity from three experiments. Red box indicates BLM region required for interaction with SMC2. b Alignment of BLM residues 150-184 with BLM from other vertebrates. Residues W154, M157, and F160 were mutated to lysine, referred to as BLM-WMF mut . c SEAP activity detected in M2H assay between two independently generated pVP16-BLM-WMF mut clones (#1, #2) and pM-SMC2. pM3-VP16 is a positive control from the manufacturer expressing a fusion of the GAL4 DNA-binding domain to the VP16 activation domain. Significance of differences between means ± SD was determined by a t -test and is reported as **** p ≤ 0.0001. d Plasmid expressing BLM-WMF mut was stably transfected into BLM-KO cells. Western blot of nuclear extracts from two independently generated BLM-WMF mut clones (#1, #2) and of WT, BLM-KO, and BLM-COMP cells was probed with BLM antibody. PCNA was used as a loading control. Expression levels were analyzed 3 h after release from G1/S arrest. e Co-immunoprecipitations of BLM and BLM-WMF mut #1 were probed with antibodies against SMC2, condensin II-specific subunit NCAPH2, and known BLM-interacting proteins. Whole-cell extracts were prepared from cells 3 h after release from G1/S arrest. f PLA using antibodies against endogenous BLM and NCAPH2 in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells 3 h after release from G1/S arrest. Scale bars, 10 μm. BLM-NCAPH2 PLA foci/nucleus were quantified (BLM-COMP, n = 102 nuclei; BLM-WMF mut #1, n = 130 nuclei; BLM-KO, n = 100 nuclei). Significance of differences was determined by a Mann–Whitney test and is reported as **** p ≤ 0.0001. For additional PLA controls, see Supplementary Fig. S .

Techniques: Activity Assay, Generated, Clone Assay, Positive Control, Expressing, Binding Assay, Activation Assay, Plasmid Preparation, Stable Transfection, Transfection, Western Blot, Control, MANN-WHITNEY

Endogenous BLM was immunoprecipitated after release from G1/S arrest in ( a ) the absence of λ protein phosphatase (λPPase) and in ( b ) the presence of λPPase and probed with antibodies against SMC2, NCAPH2, RPA, and TOP2A. Cells were synchronized by double-thymidine, released, and BLM immunoprecipitated every hour for 12 h. IgG was used as a negative control for immunoprecipitation. Endogenous BLM was immunoprecipitated after release from G1/S arrest in ( c ) the absence of λ protein phosphatase (λPPase) and in ( d ) the presence of λPPase and probed with antibodies against SMC2, SMC4, and NCAPH2. Cells were synchronized by double-thymidine, released, and BLM immunoprecipitated every hour for 12 h. IgG was used as a negative control for immunoprecipitation. Experiment was performed at least twice with similar results. e Endogenous NCAPH2 was immunoprecipitated from WT, BLM-KO, and BLM-WMF mut #1 cells and probed with antibodies against BLM, SMC2, and SMC4. Cell cultures were arrested at G1/S by double-thymidine treatment, released, and NCAPH2 immunoprecipitated every hour for 7 h. IgG was used as a negative control for immunoprecipitation. Experiment was performed twice with similar results. f Endogenous NCAPH2 and SMC2 was immunoprecipitated from the same WT lysate used for hours 3–7 in ( e ) and probed with antibodies against NCAPH2, BLM, SMC2, and SMC4. IgG was used as a negative control for immunoprecipitation. NCAPH2 immunoprecipitation was performed three times with similar results and the SMC2 reciprocal immunoprecipitation once.

Journal: Communications Biology

Article Title: Condensin II interacts with BLM helicase in S phase to maintain genome stability

doi: 10.1038/s42003-025-07916-0

Figure Lengend Snippet: Endogenous BLM was immunoprecipitated after release from G1/S arrest in ( a ) the absence of λ protein phosphatase (λPPase) and in ( b ) the presence of λPPase and probed with antibodies against SMC2, NCAPH2, RPA, and TOP2A. Cells were synchronized by double-thymidine, released, and BLM immunoprecipitated every hour for 12 h. IgG was used as a negative control for immunoprecipitation. Endogenous BLM was immunoprecipitated after release from G1/S arrest in ( c ) the absence of λ protein phosphatase (λPPase) and in ( d ) the presence of λPPase and probed with antibodies against SMC2, SMC4, and NCAPH2. Cells were synchronized by double-thymidine, released, and BLM immunoprecipitated every hour for 12 h. IgG was used as a negative control for immunoprecipitation. Experiment was performed at least twice with similar results. e Endogenous NCAPH2 was immunoprecipitated from WT, BLM-KO, and BLM-WMF mut #1 cells and probed with antibodies against BLM, SMC2, and SMC4. Cell cultures were arrested at G1/S by double-thymidine treatment, released, and NCAPH2 immunoprecipitated every hour for 7 h. IgG was used as a negative control for immunoprecipitation. Experiment was performed twice with similar results. f Endogenous NCAPH2 and SMC2 was immunoprecipitated from the same WT lysate used for hours 3–7 in ( e ) and probed with antibodies against NCAPH2, BLM, SMC2, and SMC4. IgG was used as a negative control for immunoprecipitation. NCAPH2 immunoprecipitation was performed three times with similar results and the SMC2 reciprocal immunoprecipitation once.

Techniques: Immunoprecipitation, Negative Control

a Immunofluorescence microscopy images of endogenous BLM, NCAPH2, SMC2 and EdU-labeled nascent DNA in WT cells. Nucleus is outlined in merged image and box represents ROI for magnified image. Scale bars, 10 μM and 1 μM (magnified image). Quantification of BLM, NCAPH2, and SMC2 colocalization with EdU in WT cells. Colocalization percentage was determined by counting the number of BLM, NCAPH2, or SMC2 foci that overlapped with EdU in comparison to the total number of BLM, NCAPH2, or SMC2 foci in an ROI for each nucleus. 20 nuclei were analyzed for each protein and median percentage of colocalization is reported. b SIRF assay of SMC2 in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous SMC2. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the SMC2 SIRF signal/EdU ctCF is shown for individual nuclei (BLM-COMP, n = 150 nuclei; BLM-WMF mut #1, n = 156 nuclei; BLM-KO, n = 79 nuclei) and the median presented by a horizontal line. Significance of differences between cell lines was determined using a Mann-Whitney test (ns, not significant). c SIRF assay of NCAPH2 in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous NCAPH2. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the NCAPH2 SIRF signal/EdU ctCF is shown for individual nuclei (BLM-COMP, n = 99 nuclei; BLM-WMF mut #1, n = 85 nuclei; BLM-KO, n = 85 nuclei) and the median presented by a horizontal line. Significance of differences between cell lines was determined using a Mann-Whitney test (ns, not significant). d SIRF assay of BLM in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous BLM. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the BLM SIRF signal/EdU ctCF is shown for individual nuclei (BLM-COMP, n = 120 nuclei; BLM-WMF mut #1, n = 125 nuclei; BLM-KO, n = 140 nuclei) and the median presented by a horizontal line. Significance of differences between cell lines was determined using a Mann–Whitney test and is reported as **** p ≤ 0.0001. e BLM SIRF assay in the BLM-COMP and BLM-WMF mut #1 cell lines following transfection with NCAPH2 siRNA or mock siRNA. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous BLM. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the BLM SIRF signal/EdU ctCF was calculated for each nucleus (BLM-COMP siNCAPH2, n = 102 nuclei; BLM-COMP siMock, n = 89 nuclei; BLM-WMF mut #1 siMock n = 94 nuclei) with the horizontal line representing the median. Significance of differences was determined by a Mann-Whitney test and is reported as **** p ≤ 0.0001. For additional controls for Fig. 5b–e see supplementary Fig. S . f Immunofluorescence microscopy of calyculin-induced premature chromosome condensation (PCC) in BLM-COMP, BLM-KO, and BLM-WMF mut #1 cells. Following nascent DNA labeling with EdU and chromosome spreading, EdU:biotin Click-iT was performed with biotin azide and slides were hybridized with biotin antibody and stained with DAPI. Box represents ROI for magnified image. Scale bars, 10 μM. The chromosomes of three spreads from a single experiment for each cell line were analyzed to quantify the percentage of resolved and unresolved sister chromatids.

Journal: Communications Biology

Article Title: Condensin II interacts with BLM helicase in S phase to maintain genome stability

doi: 10.1038/s42003-025-07916-0

Figure Lengend Snippet: a Immunofluorescence microscopy images of endogenous BLM, NCAPH2, SMC2 and EdU-labeled nascent DNA in WT cells. Nucleus is outlined in merged image and box represents ROI for magnified image. Scale bars, 10 μM and 1 μM (magnified image). Quantification of BLM, NCAPH2, and SMC2 colocalization with EdU in WT cells. Colocalization percentage was determined by counting the number of BLM, NCAPH2, or SMC2 foci that overlapped with EdU in comparison to the total number of BLM, NCAPH2, or SMC2 foci in an ROI for each nucleus. 20 nuclei were analyzed for each protein and median percentage of colocalization is reported. b SIRF assay of SMC2 in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous SMC2. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the SMC2 SIRF signal/EdU ctCF is shown for individual nuclei (BLM-COMP, n = 150 nuclei; BLM-WMF mut #1, n = 156 nuclei; BLM-KO, n = 79 nuclei) and the median presented by a horizontal line. Significance of differences between cell lines was determined using a Mann-Whitney test (ns, not significant). c SIRF assay of NCAPH2 in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous NCAPH2. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the NCAPH2 SIRF signal/EdU ctCF is shown for individual nuclei (BLM-COMP, n = 99 nuclei; BLM-WMF mut #1, n = 85 nuclei; BLM-KO, n = 85 nuclei) and the median presented by a horizontal line. Significance of differences between cell lines was determined using a Mann-Whitney test (ns, not significant). d SIRF assay of BLM in BLM-COMP, BLM-WMF mut #1, and BLM-KO cells. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous BLM. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the BLM SIRF signal/EdU ctCF is shown for individual nuclei (BLM-COMP, n = 120 nuclei; BLM-WMF mut #1, n = 125 nuclei; BLM-KO, n = 140 nuclei) and the median presented by a horizontal line. Significance of differences between cell lines was determined using a Mann–Whitney test and is reported as **** p ≤ 0.0001. e BLM SIRF assay in the BLM-COMP and BLM-WMF mut #1 cell lines following transfection with NCAPH2 siRNA or mock siRNA. Following nascent DNA labeling with EdU and EdU:biotin co-Click with biotin azide and Alexa Fluor 488 azide, PLA was performed using antibodies against biotin and endogenous BLM. Nucleus is outlined in the merged image. Scale bars, 10 μM. Corrected total Cellular Fluorescence (ctCF) of the BLM SIRF signal/EdU ctCF was calculated for each nucleus (BLM-COMP siNCAPH2, n = 102 nuclei; BLM-COMP siMock, n = 89 nuclei; BLM-WMF mut #1 siMock n = 94 nuclei) with the horizontal line representing the median. Significance of differences was determined by a Mann-Whitney test and is reported as **** p ≤ 0.0001. For additional controls for Fig. 5b–e see supplementary Fig. S . f Immunofluorescence microscopy of calyculin-induced premature chromosome condensation (PCC) in BLM-COMP, BLM-KO, and BLM-WMF mut #1 cells. Following nascent DNA labeling with EdU and chromosome spreading, EdU:biotin Click-iT was performed with biotin azide and slides were hybridized with biotin antibody and stained with DAPI. Box represents ROI for magnified image. Scale bars, 10 μM. The chromosomes of three spreads from a single experiment for each cell line were analyzed to quantify the percentage of resolved and unresolved sister chromatids.

Techniques: Immunofluorescence, Microscopy, Labeling, Comparison, DNA Labeling, Fluorescence, MANN-WHITNEY, Transfection, Staining

a Model of how BLM binding to condensin II increases efficiency of detection and repair of BLM substrates. Current models of loop extrusion posit that the hinge domain reels in new DNA through the SMC2-SMC4 lumen creating an intermediate loop with gate opening potentially allowing the intermediate loop to join the main loop , , , . BLM, through its interaction with condensin II at the WMF site, can scan this intermediate loop for its substrates such as R-loops, DNA breaks, or G-quadruplexes, leading to their resolution prior to becoming an impediment to the replication or transcription machinery, thus mediating normal DNA transactions and genome stability. The many DNA repair and replication factors that bind to BLM’s disordered tail likely contribute to resolution and repair. In the absence of BLM from condensin II due to the WMF mutation, the DNA lesions and replisome blocks are not resolved efficiently, thus increasing risk of collisions with the replisome or transcriptional machinery, leading to impaired replisome progression and fork stalling, impaired DNA-damage response, delayed DSB repair and, eventually, mitotic chromosome aberrations. Created in BioRender. Rodemoyer, B. (2025) https://BioRender.com/h40u746 . b Model of how BLM-condensin II interaction may contribute to suppression of crossovers. Extrusion of adjacent loops may aid BLM helicase-mediated branch migration of Holliday junctions between sister chromatids. BLM-condensin II interaction puts BLM in close proximity to the HR intermediate, increasing efficiency of dissolution as noncrossovers (NCO) in cooperation with interacting proteins. Loss of BLM-condensin II interaction due to BLM-WMF mut reduces dissolution of HR intermediates by BLM complexes and increases resolution via cleavage by structure-specific endonucleases, causing crossovers (CO). Created in BioRender. Rodemoyer, B. (2025) https://BioRender.com/k17g890 .

Journal: Communications Biology

Article Title: Condensin II interacts with BLM helicase in S phase to maintain genome stability

doi: 10.1038/s42003-025-07916-0

Figure Lengend Snippet: a Model of how BLM binding to condensin II increases efficiency of detection and repair of BLM substrates. Current models of loop extrusion posit that the hinge domain reels in new DNA through the SMC2-SMC4 lumen creating an intermediate loop with gate opening potentially allowing the intermediate loop to join the main loop , , , . BLM, through its interaction with condensin II at the WMF site, can scan this intermediate loop for its substrates such as R-loops, DNA breaks, or G-quadruplexes, leading to their resolution prior to becoming an impediment to the replication or transcription machinery, thus mediating normal DNA transactions and genome stability. The many DNA repair and replication factors that bind to BLM’s disordered tail likely contribute to resolution and repair. In the absence of BLM from condensin II due to the WMF mutation, the DNA lesions and replisome blocks are not resolved efficiently, thus increasing risk of collisions with the replisome or transcriptional machinery, leading to impaired replisome progression and fork stalling, impaired DNA-damage response, delayed DSB repair and, eventually, mitotic chromosome aberrations. Created in BioRender. Rodemoyer, B. (2025) https://BioRender.com/h40u746 . b Model of how BLM-condensin II interaction may contribute to suppression of crossovers. Extrusion of adjacent loops may aid BLM helicase-mediated branch migration of Holliday junctions between sister chromatids. BLM-condensin II interaction puts BLM in close proximity to the HR intermediate, increasing efficiency of dissolution as noncrossovers (NCO) in cooperation with interacting proteins. Loss of BLM-condensin II interaction due to BLM-WMF mut reduces dissolution of HR intermediates by BLM complexes and increases resolution via cleavage by structure-specific endonucleases, causing crossovers (CO). Created in BioRender. Rodemoyer, B. (2025) https://BioRender.com/k17g890 .

Techniques: Binding Assay, Mutagenesis, Migration, Dissolution

a Diagram of condensins I and II, which share the same SMC ATPase subunits (SMC2 and SMC4) and have distinct sets of non-SMC regulatory proteins (CAP-H, -D2, and -G for condensin I, and CAP-H2, -D3, and -G2 for condensin II). b Fluorescent images of FA-fixed HCT116 cells depleted (KD) of SMC2 (condensins I and II). Top, control HCT116 cells (DMSO vehicle only). Bottom, SMC2-mClover depleted HCT116 cells with IAA treatment. From left to right, DNA (DAPI), SMC2-mClover, and merged. c Box plots with dots of the SMC2-mClover signal intensity. A.U. means arbitrary unit. Whiskers, bounds of box and gray bars show maxima, minima, first/third quantiles, and median values. Median values of control and SMC2 KD are 1.6 × 10 3 (n = 13 cells) and 1.5 × 10 2 (n = 10 cells), respectively. ***P < 0.0001 (P = 1.7 × 10 −6 ) by Wilcoxon rank sum test (two-sided). d MSD plot (±SD among cells) of TMR-labeled interphase (Interphase, gray, n = 13 cells) and metaphase nucleosomes (Metaphase, black, n = 13 cells) in living HCT116 cells without or with condensins I and II depletion (SMC2 KD, magenta, n = 10 cells) from 0.05 to 0.5 s. The Kolmogorov-Smirnov test (two-sided) was used to determine P values. ***, P ≤ 0.0005, for with versus without SMC2 KD ( P = 1.3 × 10 −4 ), not significant (N.S.) for interphase versus metaphase with condensins KD ( P = 0.44). MSD exponents from Supplementary Fig. and AC values from Supplementary Fig. are also shown in brackets.

Journal: Nature Communications

Article Title: Single-nucleosome imaging unveils that condensins and nucleosome–nucleosome interactions differentially constrain chromatin to organize mitotic chromosomes

doi: 10.1038/s41467-024-51454-y

Figure Lengend Snippet: a Diagram of condensins I and II, which share the same SMC ATPase subunits (SMC2 and SMC4) and have distinct sets of non-SMC regulatory proteins (CAP-H, -D2, and -G for condensin I, and CAP-H2, -D3, and -G2 for condensin II). b Fluorescent images of FA-fixed HCT116 cells depleted (KD) of SMC2 (condensins I and II). Top, control HCT116 cells (DMSO vehicle only). Bottom, SMC2-mClover depleted HCT116 cells with IAA treatment. From left to right, DNA (DAPI), SMC2-mClover, and merged. c Box plots with dots of the SMC2-mClover signal intensity. A.U. means arbitrary unit. Whiskers, bounds of box and gray bars show maxima, minima, first/third quantiles, and median values. Median values of control and SMC2 KD are 1.6 × 10 3 (n = 13 cells) and 1.5 × 10 2 (n = 10 cells), respectively. ***P < 0.0001 (P = 1.7 × 10 −6 ) by Wilcoxon rank sum test (two-sided). d MSD plot (±SD among cells) of TMR-labeled interphase (Interphase, gray, n = 13 cells) and metaphase nucleosomes (Metaphase, black, n = 13 cells) in living HCT116 cells without or with condensins I and II depletion (SMC2 KD, magenta, n = 10 cells) from 0.05 to 0.5 s. The Kolmogorov-Smirnov test (two-sided) was used to determine P values. ***, P ≤ 0.0005, for with versus without SMC2 KD ( P = 1.3 × 10 −4 ), not significant (N.S.) for interphase versus metaphase with condensins KD ( P = 0.44). MSD exponents from Supplementary Fig. and AC values from Supplementary Fig. are also shown in brackets.

Article Snippet: Primary antibodies: anti-OsTIR1 (1:1000, MBL, #PD048), anti-mAID (1:1000, MBL, #M214-3), anti-SMC2 (1:1000, Bethyl, #A300-058A-T), and anti-GAPDH conjugated with rhodamine (1:5000, Bio-Rad, 12004167).

Techniques: Control, Labeling

a Illustration of the effects caused by trichostatin A (TSA) and condensin depletion (KD) . Chromosome cross-section view (top left). TSA treatment induces histone tail hyperacetylation and weakens nucleosome interactions (top right). Abnormal chromosome after condensin depletion (bottom left). TSA treatment of condensin-depleted cells results in greatly decompacted hyperacetylated chromatin, which is diffusely distributed throughout the cytoplasm (bottom right). b (left) Western blot of tail acetylated H3 and H4 from untreated (lane 1), SMC2 KD (2), 4 h TSA-treated (3) and 4 h TSA-treated SMC2 KD (4) HCT116 cells. H2B was used as a control. (right) Box plots (whiskers, maxima/minima; bounds of box, first/third quantiles) of SMC2-mClover signal. A.U. means arbitrary unit. Gray and black bars show mean and median values. Data from n = 27 (control), n = 20 (SMC2 KD), n = 24 (TSA), n = 16 (SMC2 KD + TSA) cells are shown. *** P < 0.0001 by Wilcoxon rank sum test (two-sided). c MSD plot (±SD among cells) of JF549-labeled nucleosomes in the mitotic HCT116 cells with condensins I and II depletion (SMC2 KD, blue, n = 20), condensins I and II depletion +5 µM TSA treatment (4 h) (SMC2 KD + 5 µM TSA, purple, n = 16), 5 µM TSA treatment (5 µM TSA, magenta, n = 24), and untreated control (control, black, n = 27). The Kolmogorov-Smirnov test (two-sided) was used. *** P ≤ 0.0005 for control versus SMC2 KD + 5 µM TSA ( P = 7.5 × 10 −12 ), control versus SMC2 KD ( P = 2.2 × 10 −8 ), control versus 5 µM TSA ( P = 2.4 × 10 −7 ). Not significant (N.S.) for SMC2 KD versus 5 µM TSA ( P = 0.11). MSD exponents and AC values from Supplementary Fig. are also shown. d Fluorescent images of FA-fixed HCT116 cells with SMC2-mAID-mClover expressing H2B-Halo; H2B-Halo-JF549 (top), SMC2-mClover (middle), and merged images (bottom). From left to right, untreated control, condensins I and II depleted cell with IAA addition, TSA-treated cell, and TSA-treated cell with condensins I and II depletion.

Journal: Nature Communications

Article Title: Single-nucleosome imaging unveils that condensins and nucleosome–nucleosome interactions differentially constrain chromatin to organize mitotic chromosomes

doi: 10.1038/s41467-024-51454-y

Figure Lengend Snippet: a Illustration of the effects caused by trichostatin A (TSA) and condensin depletion (KD) . Chromosome cross-section view (top left). TSA treatment induces histone tail hyperacetylation and weakens nucleosome interactions (top right). Abnormal chromosome after condensin depletion (bottom left). TSA treatment of condensin-depleted cells results in greatly decompacted hyperacetylated chromatin, which is diffusely distributed throughout the cytoplasm (bottom right). b (left) Western blot of tail acetylated H3 and H4 from untreated (lane 1), SMC2 KD (2), 4 h TSA-treated (3) and 4 h TSA-treated SMC2 KD (4) HCT116 cells. H2B was used as a control. (right) Box plots (whiskers, maxima/minima; bounds of box, first/third quantiles) of SMC2-mClover signal. A.U. means arbitrary unit. Gray and black bars show mean and median values. Data from n = 27 (control), n = 20 (SMC2 KD), n = 24 (TSA), n = 16 (SMC2 KD + TSA) cells are shown. *** P < 0.0001 by Wilcoxon rank sum test (two-sided). c MSD plot (±SD among cells) of JF549-labeled nucleosomes in the mitotic HCT116 cells with condensins I and II depletion (SMC2 KD, blue, n = 20), condensins I and II depletion +5 µM TSA treatment (4 h) (SMC2 KD + 5 µM TSA, purple, n = 16), 5 µM TSA treatment (5 µM TSA, magenta, n = 24), and untreated control (control, black, n = 27). The Kolmogorov-Smirnov test (two-sided) was used. *** P ≤ 0.0005 for control versus SMC2 KD + 5 µM TSA ( P = 7.5 × 10 −12 ), control versus SMC2 KD ( P = 2.2 × 10 −8 ), control versus 5 µM TSA ( P = 2.4 × 10 −7 ). Not significant (N.S.) for SMC2 KD versus 5 µM TSA ( P = 0.11). MSD exponents and AC values from Supplementary Fig. are also shown. d Fluorescent images of FA-fixed HCT116 cells with SMC2-mAID-mClover expressing H2B-Halo; H2B-Halo-JF549 (top), SMC2-mClover (middle), and merged images (bottom). From left to right, untreated control, condensins I and II depleted cell with IAA addition, TSA-treated cell, and TSA-treated cell with condensins I and II depletion.

Techniques: Western Blot, Control, Labeling, Expressing

a Upper, cartoon depiction of nucleosomes inside or outside the chromosomal axis. Image 1, enhanced SMC2-mClover region, which corresponds to the axis; image 2, extracted axis region (yellow dashed line) and nucleosome dots. b MSD plot (±SD among cells) of TMR-labeled nucleosomes inside (axis, solid blue, n = 14) and outside (periphery, solid magenta, n = 14) the SMC2-mClover enriched axis regions of mitotic chromosomes in TSA-treated HCT116 cells (0.05 to 0.5 s). The MSD data without TSA treatment are shown as dashed lines [axis, blue (n = 18); periphery, magenta (n = 18)], which almost overlap the inside axis of TSA-treated chromosomes. ***, P ≤ 0.0005, Kolmogorov–Smirnov test (two-sided) for TSA peripheral versus TSA axis regions ( P = 1.9 × 10 −5 ). N.S. for TSA axis regions versus non-TSA treated axis ( P = 0.33) or peripheral ( P = 0.15) regions. MSD exponents from Supplementary Fig. and AC values from Supplementary Fig. are also shown in the brackets. c Nucleosomes around the periphery (those mostly free from condensins) in the TSA-treated chromosomes, whose nucleosome–nucleosomes interactions were weakened, were less constrained and had higher mobility than those around the axis.

Journal: Nature Communications

Article Title: Single-nucleosome imaging unveils that condensins and nucleosome–nucleosome interactions differentially constrain chromatin to organize mitotic chromosomes

doi: 10.1038/s41467-024-51454-y

Figure Lengend Snippet: a Upper, cartoon depiction of nucleosomes inside or outside the chromosomal axis. Image 1, enhanced SMC2-mClover region, which corresponds to the axis; image 2, extracted axis region (yellow dashed line) and nucleosome dots. b MSD plot (±SD among cells) of TMR-labeled nucleosomes inside (axis, solid blue, n = 14) and outside (periphery, solid magenta, n = 14) the SMC2-mClover enriched axis regions of mitotic chromosomes in TSA-treated HCT116 cells (0.05 to 0.5 s). The MSD data without TSA treatment are shown as dashed lines [axis, blue (n = 18); periphery, magenta (n = 18)], which almost overlap the inside axis of TSA-treated chromosomes. ***, P ≤ 0.0005, Kolmogorov–Smirnov test (two-sided) for TSA peripheral versus TSA axis regions ( P = 1.9 × 10 −5 ). N.S. for TSA axis regions versus non-TSA treated axis ( P = 0.33) or peripheral ( P = 0.15) regions. MSD exponents from Supplementary Fig. and AC values from Supplementary Fig. are also shown in the brackets. c Nucleosomes around the periphery (those mostly free from condensins) in the TSA-treated chromosomes, whose nucleosome–nucleosomes interactions were weakened, were less constrained and had higher mobility than those around the axis.

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