AI Article Synopsis
- TFIIH is a crucial human general transcription factor that plays roles in both transcription and DNA repair.
- A specific structural domain in TFIIH's core subunit, p62, is essential for its DNA repair function through the nucleotide excision repair pathway, particularly involving its interaction with the XPG endonuclease.
- Research revealed that while the N-terminal domain of p62 is vital for DNA repair, it is not necessary for the assembly of the TFIIH complex or basic transcription, and a new structural feature was identified that indicates a novel type of activity.
Article Abstract
The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold.
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| http://dx.doi.org/10.1038/nsmb782 | DOI Listing |
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