The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.

ABSTRACT: Nucleotide excision repair (NER) is the key pathway for the removal of DNA damage induced by UV irradiation and chemotherapeutic reagents. Protein-protein interactions are crucial for the dynamic and coordinated assembly of the proteins involved in DNA lesions. Here we focus on the role of interactions between the multi-subunit helicase/translocase complex TFIIH and the 3' endonuclease XPG. We show that XPG interacts with the p62 and XPD subunits of TFIIH through its long spacer region bridging its split active site. We show that interactions between three acidic regions of XPG and the Pleckstrin homology (PH) domain of p62 are of moderate importance for NER, while defects in the interactions with XPD fail to pull-down TFIIH and strongly reduce NER activity. These p62 and XPD interface mut

SUBMITTER: Kim M 

PROVIDER: S-EPMC12873601 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature