Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair.
作者： Frédéric Coin , Valentyn Oksenych , Jean-Marc Egly
DOI: 10.1016/J.MOLCEL.2007.03.009
关键词: Biology 、 Xeroderma pigmentosum 、 Transcription (biology) 、 Nucleotide excision repair 、 Helicase 、 Transcription Factor TFIIH 、 Transcription factor II H 、 DNA repair 、 DNA damage 、 Molecular biology
摘要: Mutations in XPB, an essential subunit of the transcription/repair factor TFIIH, lead to nucleotide excision repair (NER) defects and xeroderma pigmentosum (XP). The role XPB NER molecular mechanisms resulting XP are poorly understood. Here, we show that p52 TFIIH interacts with stimulates its ATPase activity. A mutation found among XP-B patients (F99S) weakens this interaction stimulation, thereby explaining defect damaged DNA opening. We next mutations helicase motifs III (T469A) VI (Q638A) inhibit activity preserve function TFIIH. Our results suggest a mechanism which is not used for opening DNA, instead only driven by activity, combination XPD.
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