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GenScript corporation full-length coding sequence of human c6orf106 np_077270.1

Validation of <t>C6orf106</t> knockdown and overexpression in HeLa cells. a and b, HeLa cells were transfected with siRNAs targeting C6orf106 (siC6orf106) or a nontargeting control (siNEG) and assayed by qRT-PCR (a) or Western blotting (b) for C6orf106 expression levels. c, validation of C6orf106-FLAG expression by Western blotting. d, cell viability in HeLa cells treated with the indicated siRNAs or cDNAs. Values are normalized against cells treated with transfection reagent only (mock). Error bars for all graphs indicate ±1 S.D. of a minimum of three independent experiments; asterisks show significant differences as assessed by one-way ANOVA with Bonferroni post-test (*, p < 0.05; **, p < 0.01).

Full Length Coding Sequence Of Human C6orf106 Np 077270.1, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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full-length coding sequence of human c6orf106 np_077270.1 - by Bioz Stars, 2026-08

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1) Product Images from "C6orf106 is a novel inhibitor of the interferon-regulatory factor 3–dependent innate antiviral response"

Article Title: C6orf106 is a novel inhibitor of the interferon-regulatory factor 3–dependent innate antiviral response

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.RA117.001491

Validation of C6orf106 knockdown and overexpression in HeLa cells. a and b, HeLa cells were transfected with siRNAs targeting C6orf106 (siC6orf106) or a nontargeting control (siNEG) and assayed by qRT-PCR (a) or Western blotting (b) for C6orf106 expression levels. c, validation of C6orf106-FLAG expression by Western blotting. d, cell viability in HeLa cells treated with the indicated siRNAs or cDNAs. Values are normalized against cells treated with transfection reagent only (mock). Error bars for all graphs indicate ±1 S.D. of a minimum of three independent experiments; asterisks show significant differences as assessed by one-way ANOVA with Bonferroni post-test (*, p < 0.05; **, p < 0.01).

Figure Legend Snippet: Validation of C6orf106 knockdown and overexpression in HeLa cells. a and b, HeLa cells were transfected with siRNAs targeting C6orf106 (siC6orf106) or a nontargeting control (siNEG) and assayed by qRT-PCR (a) or Western blotting (b) for C6orf106 expression levels. c, validation of C6orf106-FLAG expression by Western blotting. d, cell viability in HeLa cells treated with the indicated siRNAs or cDNAs. Values are normalized against cells treated with transfection reagent only (mock). Error bars for all graphs indicate ±1 S.D. of a minimum of three independent experiments; asterisks show significant differences as assessed by one-way ANOVA with Bonferroni post-test (*, p < 0.05; **, p < 0.01).

Techniques Used: Biomarker Discovery, Knockdown, Over Expression, Transfection, Control, Quantitative RT-PCR, Western Blot, Expressing

C6orf106 suppresses antiviral cytokine synthesis. a, HeLa cells were treated with transfected poly(I:C) for 6 h, and the cells were collected and analyzed for mRNA expression of the listed cytokines by qRT-PCR. b, relative cytokine mRNA levels in HeLa cells stimulated with poly(I:C) 48 h post-transfection with siRNAs. c, relative mRNA levels in HeLa cells stimulated with poly(I:C) 24 h post-transfection with cDNAs. d, cell culture supernatants from c were assayed for IFN-β using ELISA. Relative cytokine mRNA levels in HeLa cells infected with SeV (400 hemagglutination units/well) post-transfection with siRNAs (e) or cDNA plasmids (f) are shown. g, HeLa cells were stimulated with 2000 enzyme units/ml IFN-α for 6 h, and ISG15 mRNA expression was determined by qRT-PCR. h, HeLa cells were stimulated with 20 ng/ml TNFα for 6 h, and IκBα mRNA expression was determined by qRT-PCR. i and j, HeLa cells were transfected with siRNAs (i) or cDNA plasmids (j) and then stimulated with poly(I:C) for the times shown. Relative mRNA levels of IFN-β over time were measured by qRT-PCR. k, mock cells were stimulated with poly(I:C) for the times shown, and endogenous C6orf106 and IFN-β mRNA levels were measured by qRT-PCR. Error bars indicate ±1 S.D. of three independent experiments, and asterisks show significant changes compared with controls as measured by one- or two-way ANOVA with Bonferroni post-test (***, p < 0.001; **, p < 0.01; *, p < 0.05 compared with 4 h).

Figure Legend Snippet: C6orf106 suppresses antiviral cytokine synthesis. a, HeLa cells were treated with transfected poly(I:C) for 6 h, and the cells were collected and analyzed for mRNA expression of the listed cytokines by qRT-PCR. b, relative cytokine mRNA levels in HeLa cells stimulated with poly(I:C) 48 h post-transfection with siRNAs. c, relative mRNA levels in HeLa cells stimulated with poly(I:C) 24 h post-transfection with cDNAs. d, cell culture supernatants from c were assayed for IFN-β using ELISA. Relative cytokine mRNA levels in HeLa cells infected with SeV (400 hemagglutination units/well) post-transfection with siRNAs (e) or cDNA plasmids (f) are shown. g, HeLa cells were stimulated with 2000 enzyme units/ml IFN-α for 6 h, and ISG15 mRNA expression was determined by qRT-PCR. h, HeLa cells were stimulated with 20 ng/ml TNFα for 6 h, and IκBα mRNA expression was determined by qRT-PCR. i and j, HeLa cells were transfected with siRNAs (i) or cDNA plasmids (j) and then stimulated with poly(I:C) for the times shown. Relative mRNA levels of IFN-β over time were measured by qRT-PCR. k, mock cells were stimulated with poly(I:C) for the times shown, and endogenous C6orf106 and IFN-β mRNA levels were measured by qRT-PCR. Error bars indicate ±1 S.D. of three independent experiments, and asterisks show significant changes compared with controls as measured by one- or two-way ANOVA with Bonferroni post-test (***, p < 0.001; **, p < 0.01; *, p < 0.05 compared with 4 h).

Techniques Used: Transfection, Expressing, Quantitative RT-PCR, Cell Culture, Enzyme-linked Immunosorbent Assay, Infection

C6orf106 predominantly targets IRF-driven transcription. HeLa cells were transfected with siRNAs for 24 h, then transfected with ISRE- (a) or NF-κB-firefly luciferase (luc) (b) and Renilla luciferase vectors for 20 h, and then stimulated with poly(I:C) for 6 h. Alternatively, HeLa cells were transfected with GFP or C6orf106-FLAG and ISRE- (c) or NF-κB-firefly luciferase (d) and Renilla luciferase vectors for 20 h and then stimulated with poly(I:C) for 6 h. All cell lysates were assayed for luciferase activity, normalized to the transfection control Renilla luciferase. Error bars indicate ±1 S.D. of triplicate experiments; asterisks indicate significant differences as determined by Student's t test (*, p < 0.05; **, p < 0.01).

Figure Legend Snippet: C6orf106 predominantly targets IRF-driven transcription. HeLa cells were transfected with siRNAs for 24 h, then transfected with ISRE- (a) or NF-κB-firefly luciferase (luc) (b) and Renilla luciferase vectors for 20 h, and then stimulated with poly(I:C) for 6 h. Alternatively, HeLa cells were transfected with GFP or C6orf106-FLAG and ISRE- (c) or NF-κB-firefly luciferase (d) and Renilla luciferase vectors for 20 h and then stimulated with poly(I:C) for 6 h. All cell lysates were assayed for luciferase activity, normalized to the transfection control Renilla luciferase. Error bars indicate ±1 S.D. of triplicate experiments; asterisks indicate significant differences as determined by Student's t test (*, p < 0.05; **, p < 0.01).

Techniques Used: Transfection, Luciferase, Activity Assay, Control

$C6orf106 does not impair activation or nuclear translocation of IRF3 and NF-κB. a, HeLa cells transfected with GFP or C6orf106-FLAG for 20 h were stimulated with poly(I:C) for 6 h and then lysed, and cellular proteins were separated into cytosolic and nuclear fractions. Fractions were probed for the transcription factors IRF3 and p65 as well as C6orf106 and the loading controls GAPDH (cytosol) and fibrillarin (nucleus). b, HeLa cells as in a were fixed and labeled for C6orf106-FLAG (green), IRF3 (left panel) or p65 (right panel), and nuclei (blue). White scale bars, 10 μm. c, Fn/c ratios for treatment groups shown in b. Error bars indicate ±1 S.D. of a typical experiment from duplicate experiments; asterisks indicate significant differences as determined by one-way ANOVA with Dunn's multiple comparison test (***, p < 0.001).$
Figure Legend Snippet: C6orf106 does not impair activation or nuclear translocation of IRF3 and NF-κB. a, HeLa cells transfected with GFP or C6orf106-FLAG for 20 h were stimulated with poly(I:C) for 6 h and then lysed, and cellular proteins were separated into cytosolic and nuclear fractions. Fractions were probed for the transcription factors IRF3 and p65 as well as C6orf106 and the loading controls GAPDH (cytosol) and fibrillarin (nucleus). b, HeLa cells as in a were fixed and labeled for C6orf106-FLAG (green), IRF3 (left panel) or p65 (right panel), and nuclei (blue). White scale bars, 10 μm. c, Fn/c ratios for treatment groups shown in b. Error bars indicate ±1 S.D. of a typical experiment from duplicate experiments; asterisks indicate significant differences as determined by one-way ANOVA with Dunn's multiple comparison test (***, p < 0.001).

Techniques Used: Activation Assay, Translocation Assay, Transfection, Labeling, Comparison

C6orf106 does not alter cellular protein levels of IRF3 and NF-κB. HeLa cells were transfected with cDNAs for 20 h (a) or siRNAs for 40 h (b). Cells were then pretreated for 1 h with CHX (20 μg/ml) or MG132 (10 μm) and then stimulated with poly(I:C) for 6 h. Cells were lysed, and cellular levels of IRF3, p65, and C6orf106 (endogenous or FLAG-tagged) were measured by Western blotting. c, immunoblot showing expression levels of cyclin B1 and actin in HeLa cells treated for the indicated times with CHX (20 μg/ml) or MG132 (10 μm).

Figure Legend Snippet: C6orf106 does not alter cellular protein levels of IRF3 and NF-κB. HeLa cells were transfected with cDNAs for 20 h (a) or siRNAs for 40 h (b). Cells were then pretreated for 1 h with CHX (20 μg/ml) or MG132 (10 μm) and then stimulated with poly(I:C) for 6 h. Cells were lysed, and cellular levels of IRF3, p65, and C6orf106 (endogenous or FLAG-tagged) were measured by Western blotting. c, immunoblot showing expression levels of cyclin B1 and actin in HeLa cells treated for the indicated times with CHX (20 μg/ml) or MG132 (10 μm).

Techniques Used: Transfection, Western Blot, Expressing

C6orf106 interacts with IRF3 and inhibits binding to its DNA consensus sequence. HeLa cells were transfected with cDNAs and stimulated with poly(I:C), and the nuclear proteins were extracted using a hypotonic lysis method. Nuclear proteins (10 μg) were analyzed for IRF3–DNA (a) or p65–DNA (c) binding. Alternatively, HeLa cells depleted of C6orf106 were stimulated with poly(I:C), and nuclear proteins were analyzed for IRF3–DNA (b) or p65–DNA (d) binding. e, HEK293T cells transfected with IRF3 alone or in combination with C6orf106 were stimulated with poly(I:C), lysed, and subjected to indirect immunoprecipitation with an anti-IRF3 antibody. Immunoprecipitated (IP) samples and input controls were probed with anti-FLAG antibody for Western blotting. An IgG isotype was used as a negative control for the immunoprecipitation experiment. Error bars indicate ±1 S.D. of triplicate experiments; asterisks indicate significant differences as determined by two-way ANOVA with Bonferroni post-test (***, p < 0.001; **, p < 0.01; ns, not significant).

Figure Legend Snippet: C6orf106 interacts with IRF3 and inhibits binding to its DNA consensus sequence. HeLa cells were transfected with cDNAs and stimulated with poly(I:C), and the nuclear proteins were extracted using a hypotonic lysis method. Nuclear proteins (10 μg) were analyzed for IRF3–DNA (a) or p65–DNA (c) binding. Alternatively, HeLa cells depleted of C6orf106 were stimulated with poly(I:C), and nuclear proteins were analyzed for IRF3–DNA (b) or p65–DNA (d) binding. e, HEK293T cells transfected with IRF3 alone or in combination with C6orf106 were stimulated with poly(I:C), lysed, and subjected to indirect immunoprecipitation with an anti-IRF3 antibody. Immunoprecipitated (IP) samples and input controls were probed with anti-FLAG antibody for Western blotting. An IgG isotype was used as a negative control for the immunoprecipitation experiment. Error bars indicate ±1 S.D. of triplicate experiments; asterisks indicate significant differences as determined by two-way ANOVA with Bonferroni post-test (***, p < 0.001; **, p < 0.01; ns, not significant).

Techniques Used: Binding Assay, Sequencing, Transfection, Lysis, Immunoprecipitation, Western Blot, Negative Control

$C6orf106 reduces nuclear levels of the transactivator proteins p300 and CBP. Nuclear and cytosolic fractions were isolated from HeLa cells expressing C6orf106-FLAG (a) or knocked down with siRNAs targeting C6orf106 (b) and stimulated with poly(I:C) as shown. Equal amounts of nuclear lysates were probed for members of the enhanceosome complex as shown. c, cytosolic fractions were also probed for the nuclear transactivators CBP/p300.$
Figure Legend Snippet: C6orf106 reduces nuclear levels of the transactivator proteins p300 and CBP. Nuclear and cytosolic fractions were isolated from HeLa cells expressing C6orf106-FLAG (a) or knocked down with siRNAs targeting C6orf106 (b) and stimulated with poly(I:C) as shown. Equal amounts of nuclear lysates were probed for members of the enhanceosome complex as shown. c, cytosolic fractions were also probed for the nuclear transactivators CBP/p300.

Techniques Used: Isolation, Expressing

Figure Legend Snippet: Working model of C6orf106 (C6)-mediated inhibition of IRF3-dependent cytokine transcription.

Techniques Used: Inhibition

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Silencing of GmMEKK2 by virus‐induced gene silencing (VIGS) increased soybean mosaic virus (SMV) susceptibility. (A) Efficiency of GmMEKK2 silencing in empty vector control (EV) and GmMEKK2 ‐silenced mekk2 i1 and mekk2 i2 plants at 0, 7, 14 and 21 days post‐inoculation (dpi). (B) Phenotypes of soybean after SMV infection: EV and GmMEKK2 ‐silenced lines generated using VIGS. Images were taken at 21 dpi. (C) Disease indices of plants at 21 dpi. Lowercase letters denote statistically significant differences among groups at the same time point ( p < 0.05, one‐way ANOVA with Duncan's test). (D) Relative SMV accumulation in top new leaves of EV and GmMEKK2 ‐silenced plants at 7, 14 and 21 dpi, quantified by reverse transcription‐quantitative PCR using SMV coat protein‐specific primers.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Silencing of GmMEKK2 by virus‐induced gene silencing (VIGS) increased soybean mosaic virus (SMV) susceptibility. (A) Efficiency of GmMEKK2 silencing in empty vector control (EV) and GmMEKK2 ‐silenced mekk2 i1 and mekk2 i2 plants at 0, 7, 14 and 21 days post‐inoculation (dpi). (B) Phenotypes of soybean after SMV infection: EV and GmMEKK2 ‐silenced lines generated using VIGS. Images were taken at 21 dpi. (C) Disease indices of plants at 21 dpi. Lowercase letters denote statistically significant differences among groups at the same time point ( p < 0.05, one‐way ANOVA with Duncan's test). (D) Relative SMV accumulation in top new leaves of EV and GmMEKK2 ‐silenced plants at 7, 14 and 21 dpi, quantified by reverse transcription‐quantitative PCR using SMV coat protein‐specific primers.

Article Snippet: The GmMEKK2 full‐length coding DNA sequence (CDS) was inserted into pDONOR221 (Invitrogen) and then transferred to a pB7FWG2 vector via an LR recombination reaction in the Gateway system.

Techniques: Virus, Plasmid Preparation, Control, Infection, Generated, Reverse Transcription, Real-time Polymerase Chain Reaction

Overexpression of GmMEKK2 improved soybean mosaic virus (SMV) resistance in soybean. (A) Infection symptoms on soybean leaves after SMV inoculation. NT, nontransgenic plants; ZMP1, 3, 6 and 7 indicate GmMEKK2 ‐overexpression lines 1, 3, 6 and 7, respectively. (B) Disease indices of NT and each GmMEKK2 ‐overexpression line. The disease index was investigated at 21 days post‐SMV‐inoculation. (C) Quantification of SMV content in soybean leaves. SMV‐susceptible line 1138‐2 was used as a positive control. (D) The GmMEKK2 expression pattern in NT plants after SMV inoculation. (E) Comparison of yield traits between NT and overexpression plants after SMV infection. Mock‐inoculated plants served as the control. Values labelled with different lowercase letters (a–e) are significantly different at p < 0.05 as determined by Duncan's test.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Overexpression of GmMEKK2 improved soybean mosaic virus (SMV) resistance in soybean. (A) Infection symptoms on soybean leaves after SMV inoculation. NT, nontransgenic plants; ZMP1, 3, 6 and 7 indicate GmMEKK2 ‐overexpression lines 1, 3, 6 and 7, respectively. (B) Disease indices of NT and each GmMEKK2 ‐overexpression line. The disease index was investigated at 21 days post‐SMV‐inoculation. (C) Quantification of SMV content in soybean leaves. SMV‐susceptible line 1138‐2 was used as a positive control. (D) The GmMEKK2 expression pattern in NT plants after SMV inoculation. (E) Comparison of yield traits between NT and overexpression plants after SMV infection. Mock‐inoculated plants served as the control. Values labelled with different lowercase letters (a–e) are significantly different at p < 0.05 as determined by Duncan's test.

Techniques: Over Expression, Virus, Infection, Positive Control, Expressing, Comparison, Control

Expression profiles of key differentially expressed genes (DEGs) between nontransgenic (NT) and GmMEKK2 ‐overexpression lines (ZMP) involved in the reactive oxygen species (ROS)‐ and salicylic acid (SA)‐related pathways. (A) KEGG enrichment analysis of DEGs between NT and ZMP plants. Left: NT_CK versus ZMP_CK (uninfected controls); Right: NT_7d versus ZMP_7d (7 days post‐SMV‐inoculation [dpi]). Points represent enriched pathways, with size indicating gene count and colour reflecting −log 10 (adjusted p ‐value). Red arrows highlight defence‐related pathways. (B) Expression dynamics of key components among MAPK, plant hormone signalling and plant–pathogen interaction pathways. Schematic depicts signal transduction from apoplast to cytoplasm, including Ca 2+ sensors (CNGCs and CDPKs), ROS producers (Rbohs) and SA‐induced defence protein (PR1). Heatmaps show expression levels across conditions (NT and ZMP at 0, 7 and 14 dpi), with gene IDs labelled.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Expression profiles of key differentially expressed genes (DEGs) between nontransgenic (NT) and GmMEKK2 ‐overexpression lines (ZMP) involved in the reactive oxygen species (ROS)‐ and salicylic acid (SA)‐related pathways. (A) KEGG enrichment analysis of DEGs between NT and ZMP plants. Left: NT_CK versus ZMP_CK (uninfected controls); Right: NT_7d versus ZMP_7d (7 days post‐SMV‐inoculation [dpi]). Points represent enriched pathways, with size indicating gene count and colour reflecting −log 10 (adjusted p ‐value). Red arrows highlight defence‐related pathways. (B) Expression dynamics of key components among MAPK, plant hormone signalling and plant–pathogen interaction pathways. Schematic depicts signal transduction from apoplast to cytoplasm, including Ca 2+ sensors (CNGCs and CDPKs), ROS producers (Rbohs) and SA‐induced defence protein (PR1). Heatmaps show expression levels across conditions (NT and ZMP at 0, 7 and 14 dpi), with gene IDs labelled.

Techniques: Expressing, Over Expression, Transduction

Kinase activity of GmMEKK2 is dispensable for its function in mediating defence signalling. (A–E) Relative expression levels of (A) GmMKK1 , (B) GmMPK4A , (C) GmMPK13‐like , (D) GmSUMM2 and (E) GmCRCK3 in nontransgenic control (NT), GmMEKK2 ‐overexpression lines (ZMP1, ZMP3 and ZMP7), empty vector control (EV) and GmMEKK2‐ silenced lines ( mekk2 i1 and mekk2 i2 ). Lowercase letters denote significant differences at p < 0.05 as determined by one‐way ANOVA with Duncan's test. (F) Domain architecture of GmMEKK2 highlighting the kinase domain (6–264 amino acids) and ATP‐binding site (K36). Autophosphorylation of GmMEKK2 was assessed by immunoblotting with α‐pSer/Thr antibody. Recombinant proteins GmMEKK1‐FLAG and GmMEKK1 K321M ‐FLAG were used as positive and negative controls, respectively. Coomassie brilliant blue staining validated the equal loading of recombinant proteins. (G) Yeast two‐hybrid analysis of GmMEKK2 interaction with GmMKK1, GmMPK4A and GmMPK13‐like. Transformants expressing pGADT7 and pGBKT7 constructs were grown on SD/−Leu/−Trp (control) and SD/−Leu/−Trp/−Ade/−His (selection) media. (H–J) Glutathione S‐transferase (GST) pull‐down assays with anti‐His and anti‐GST antibodies demonstrating direct binding between GST‐GmMEKK2 and (H) GmMKK1‐His, (I) GmMPK4A‐His and (J) GmMPK13‐like‐His.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Kinase activity of GmMEKK2 is dispensable for its function in mediating defence signalling. (A–E) Relative expression levels of (A) GmMKK1 , (B) GmMPK4A , (C) GmMPK13‐like , (D) GmSUMM2 and (E) GmCRCK3 in nontransgenic control (NT), GmMEKK2 ‐overexpression lines (ZMP1, ZMP3 and ZMP7), empty vector control (EV) and GmMEKK2‐ silenced lines ( mekk2 i1 and mekk2 i2 ). Lowercase letters denote significant differences at p < 0.05 as determined by one‐way ANOVA with Duncan's test. (F) Domain architecture of GmMEKK2 highlighting the kinase domain (6–264 amino acids) and ATP‐binding site (K36). Autophosphorylation of GmMEKK2 was assessed by immunoblotting with α‐pSer/Thr antibody. Recombinant proteins GmMEKK1‐FLAG and GmMEKK1 K321M ‐FLAG were used as positive and negative controls, respectively. Coomassie brilliant blue staining validated the equal loading of recombinant proteins. (G) Yeast two‐hybrid analysis of GmMEKK2 interaction with GmMKK1, GmMPK4A and GmMPK13‐like. Transformants expressing pGADT7 and pGBKT7 constructs were grown on SD/−Leu/−Trp (control) and SD/−Leu/−Trp/−Ade/−His (selection) media. (H–J) Glutathione S‐transferase (GST) pull‐down assays with anti‐His and anti‐GST antibodies demonstrating direct binding between GST‐GmMEKK2 and (H) GmMKK1‐His, (I) GmMPK4A‐His and (J) GmMPK13‐like‐His.

Techniques: Activity Assay, Expressing, Control, Over Expression, Plasmid Preparation, Binding Assay, Western Blot, Recombinant, Staining, Construct, Selection

GmMEKK2 promotes the immune response induced by salicylic acid (SA). (A) Contents of free (SA) and bound salicylic acid (SAG) in nontransgenic (NT) and GmMEKK2 ‐overexpression (ZMP) lines. (B) GmMEKK2 expression in NT plants after exogenous hormone treatments. ETH, ethylene; ABA, abscisic acid (C–H) Expression of pivotal genes in the SA signalling pathway in NT, GmMEKK2 ‐overexpression and GmMEKK2 ‐silenced ( mekk2 i1 and mekk2 i2 ) plants at 7 days post‐inoculation. EV, empty vector. Values labelled with different lowercase letters (a–c) are significantly different at p < 0.05 as determined by Duncan's test.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: GmMEKK2 promotes the immune response induced by salicylic acid (SA). (A) Contents of free (SA) and bound salicylic acid (SAG) in nontransgenic (NT) and GmMEKK2 ‐overexpression (ZMP) lines. (B) GmMEKK2 expression in NT plants after exogenous hormone treatments. ETH, ethylene; ABA, abscisic acid (C–H) Expression of pivotal genes in the SA signalling pathway in NT, GmMEKK2 ‐overexpression and GmMEKK2 ‐silenced ( mekk2 i1 and mekk2 i2 ) plants at 7 days post‐inoculation. EV, empty vector. Values labelled with different lowercase letters (a–c) are significantly different at p < 0.05 as determined by Duncan's test.

Techniques: Over Expression, Expressing, Plasmid Preparation

GmMEKK2 is involved in the regulation of reactive oxygen species homeostasis in soybean. (A, B) H 2 O 2 and O 2− levels in leaves were detected at 7 days post‐inoculation (dpi) using 3,3′‐diaminobenzidine (DAB) and nitroblue tetrazolium (NBT) staining, respectively. The mock‐inoculated leaves were sampled as controls. (C–G) Trends in the gene expression of antioxidases were measured after soybean mosaic virus (SMV) infection. CK, noninoculated control (H–J) Antioxidase activities were measured. POD, peroxidase; CAT, catalase; SOD, superoxide dismutase. The statistical analysis was independently performed for GmMEKK2 ‐overexpression lines ZMP1, ZMP3 and ZMP7, and gene‐silenced lines mekk2 i1 , mekk2 i2 and nontransgenic (NT) plants at each stage. Values labelled with different lowercase letters are significantly different at p < 0.05 as determined by Duncan's test.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: GmMEKK2 is involved in the regulation of reactive oxygen species homeostasis in soybean. (A, B) H 2 O 2 and O 2− levels in leaves were detected at 7 days post‐inoculation (dpi) using 3,3′‐diaminobenzidine (DAB) and nitroblue tetrazolium (NBT) staining, respectively. The mock‐inoculated leaves were sampled as controls. (C–G) Trends in the gene expression of antioxidases were measured after soybean mosaic virus (SMV) infection. CK, noninoculated control (H–J) Antioxidase activities were measured. POD, peroxidase; CAT, catalase; SOD, superoxide dismutase. The statistical analysis was independently performed for GmMEKK2 ‐overexpression lines ZMP1, ZMP3 and ZMP7, and gene‐silenced lines mekk2 i1 , mekk2 i2 and nontransgenic (NT) plants at each stage. Values labelled with different lowercase letters are significantly different at p < 0.05 as determined by Duncan's test.

Techniques: Staining, Gene Expression, Virus, Infection, Control, Over Expression

Molecular mechanisms underlying the GmMEKK2‐mediated regulation of soybean mosaic virus (SMV) resistance in soybean. (A) Phenotype and regulatory mechanism of GmMEKK2 ‐overexpression plants under SMV inoculation. Left: GmMEKK2 ‐overexpression plants (ZMP) show no visible SMV symptoms with autoimmunity phenotype such as leaf yellowing. Right: In ZMP plants, GmMEKK2 (orange ellipses) interacts with GmMKK1 and GmMPK4A, blocking the phosphorylation (letter P in a blue circle) of the GmMEKK1‐GmMKK1‐GmMPK4A cascade. This inhibition represses (cross in a red circle) WRKY transcription factors and leads to non‐phosphorylated CRCK3 releasing SUMM2. This then triggers defence responses such as salicylic acid (SA)‐induced gene expression and basal reactive oxygen species (ROS) accumulation. The elevated ROS constitutivly results in autoimmunity in ZMP plants. (B) Left: Nontransgenic (NT) plants exhibit severe SMV symptoms such as mosaic leaves and mottled pods. Right: In NT plants, GmMEKK2 expression is low, so the GmMEKK1‐GmMKK1‐GmMPK4A cascade remains active. GmMPK4A phosphorylates CRCK3, which binds with and represses SUMM2. This suppresses defence responses, and leads to a ROS burst.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Molecular mechanisms underlying the GmMEKK2‐mediated regulation of soybean mosaic virus (SMV) resistance in soybean. (A) Phenotype and regulatory mechanism of GmMEKK2 ‐overexpression plants under SMV inoculation. Left: GmMEKK2 ‐overexpression plants (ZMP) show no visible SMV symptoms with autoimmunity phenotype such as leaf yellowing. Right: In ZMP plants, GmMEKK2 (orange ellipses) interacts with GmMKK1 and GmMPK4A, blocking the phosphorylation (letter P in a blue circle) of the GmMEKK1‐GmMKK1‐GmMPK4A cascade. This inhibition represses (cross in a red circle) WRKY transcription factors and leads to non‐phosphorylated CRCK3 releasing SUMM2. This then triggers defence responses such as salicylic acid (SA)‐induced gene expression and basal reactive oxygen species (ROS) accumulation. The elevated ROS constitutivly results in autoimmunity in ZMP plants. (B) Left: Nontransgenic (NT) plants exhibit severe SMV symptoms such as mosaic leaves and mottled pods. Right: In NT plants, GmMEKK2 expression is low, so the GmMEKK1‐GmMKK1‐GmMPK4A cascade remains active. GmMPK4A phosphorylates CRCK3, which binds with and represses SUMM2. This suppresses defence responses, and leads to a ROS burst.

Techniques: Virus, Over Expression, Blocking Assay, Phospho-proteomics, Inhibition, Gene Expression, Expressing

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