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A. SAP25 region 16-30 is sufficient and region 21-40 is required for interaction with SCF(FBXO3). Quantitative (dNSAF) values for SAP25, SCF(FBXO3) complex subunits, and <t>SIN3A</t> are shown for Halo-SAP25 WT Halo-SAP25 16-30 and Halo-SAP25 Δ21-40purifications. Bait proteins were transiently expressed in 293T cells. Values are the average of at least three biological replicates and error bars represent standard deviation. B. FBXO3captures SAP25 but no other Sin3 complex subunits. SNAP-FLAG-FBXO3 was co-expressed with the indicated Halo-tagged proteins and the resulting lysates subjected to SNAP affinity purification. Copurified proteins were identified by SDS-PAGE followed by Western blotting using the indicated antibodies. C. Amino acid positions within SAP25 region 16-30 are important for FBXO3 capture Proteins captured by either Halo-SAP25or Halo-SAP25 S26/27/40D T35E were resolved by SDS-PAGE and detected by Western blotting using the indicated antibodies. Mutated amino acids within an N-terminal region are highlighted in red. D. Inferred position within SAP25 required for FBXO3 binding. Possible abrogation of SAP25/FBXO3 interaction by modified residues within the binding region are indicated by red Ps.
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A. SAP25 region 16-30 is sufficient and region 21-40 is required for interaction with SCF(FBXO3). Quantitative (dNSAF) values for SAP25, SCF(FBXO3) complex subunits, and SIN3A are shown for Halo-SAP25 WT Halo-SAP25 16-30 and Halo-SAP25 Δ21-40purifications. Bait proteins were transiently expressed in 293T cells. Values are the average of at least three biological replicates and error bars represent standard deviation. B. FBXO3captures SAP25 but no other Sin3 complex subunits. SNAP-FLAG-FBXO3 was co-expressed with the indicated Halo-tagged proteins and the resulting lysates subjected to SNAP affinity purification. Copurified proteins were identified by SDS-PAGE followed by Western blotting using the indicated antibodies. C. Amino acid positions within SAP25 region 16-30 are important for FBXO3 capture Proteins captured by either Halo-SAP25or Halo-SAP25 S26/27/40D T35E were resolved by SDS-PAGE and detected by Western blotting using the indicated antibodies. Mutated amino acids within an N-terminal region are highlighted in red. D. Inferred position within SAP25 required for FBXO3 binding. Possible abrogation of SAP25/FBXO3 interaction by modified residues within the binding region are indicated by red Ps.

Journal: bioRxiv

Article Title: Distinct regions within SAP25 recruit O-linked glycosylation, DNA demethylation, and ubiquitin ligase and hydrolase activities to the Sin3/HDAC complex

doi: 10.1101/2024.03.05.583553

Figure Lengend Snippet: A. SAP25 region 16-30 is sufficient and region 21-40 is required for interaction with SCF(FBXO3). Quantitative (dNSAF) values for SAP25, SCF(FBXO3) complex subunits, and SIN3A are shown for Halo-SAP25 WT Halo-SAP25 16-30 and Halo-SAP25 Δ21-40purifications. Bait proteins were transiently expressed in 293T cells. Values are the average of at least three biological replicates and error bars represent standard deviation. B. FBXO3captures SAP25 but no other Sin3 complex subunits. SNAP-FLAG-FBXO3 was co-expressed with the indicated Halo-tagged proteins and the resulting lysates subjected to SNAP affinity purification. Copurified proteins were identified by SDS-PAGE followed by Western blotting using the indicated antibodies. C. Amino acid positions within SAP25 region 16-30 are important for FBXO3 capture Proteins captured by either Halo-SAP25or Halo-SAP25 S26/27/40D T35E were resolved by SDS-PAGE and detected by Western blotting using the indicated antibodies. Mutated amino acids within an N-terminal region are highlighted in red. D. Inferred position within SAP25 required for FBXO3 binding. Possible abrogation of SAP25/FBXO3 interaction by modified residues within the binding region are indicated by red Ps.

Article Snippet: Rabbit anti-SAP30 (ab125187) and rabbit anti-SIN3A (ab3479) polyclonal antibodies were from Abcam (Cambridge, United Kingdom).

Techniques: Standard Deviation, Affinity Purification, SDS Page, Western Blot, Binding Assay, Modification