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Interplay of the Tfb1 pleckstrin homology domain with Rad2 and Rad4 in transcription coupled and global genomic nucleotide excision repair

Nucleic Acids Res. 2024-04; 
Wenzhi Gong, Hannah Holmberg, Cheng Lu, Michelle Huang, Shisheng Li
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Catalog Antibody 3 × FLAG tagged Rad2, 6 × FLAG tagged Rad4, 3 × MYC tagged Tfb1 and α-tubulin in the protein extracts were respectively detected by Western blot, using anti-FLAG (M2, Sigma), anti-MYC (A00863, Genscript), anti-tubulin (GTX76511, GeneTex) antibodies. Get A Quote

摘要

Transcription-coupled repair (TCR) and global genomic repair (GGR) are two subpathways of nucleotide excision repair (NER). The TFIIH subunit Tfb1 contains a Pleckstrin homology domain (PHD), which was shown to interact with one PHD-binding segment (PB) of Rad4 and two PHD-binding segments (PB1 and PB2) of Rad2 in vitro. Whether and how the different Rad2 and Rad4 PBs interact with the same Tfb1 PHD, and whether and how they affect TCR and GGR within the cell remain mysterious. We found that Rad4 PB constitutively interacts with Tfb1 PHD, and the two proteins may function within one module for damage recognition in TCR and GGR. Rad2 PB1 protects Tfb1 from degradation and interacts with Tfb1 PHD at a basal level... More

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