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Structural basis of TFIIH activation for nucleotide excision repair
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Structural basis of TFIIH activation for nucleotide excision repair
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Journal Article
Structural basis of TFIIH activation for nucleotide excision repair
2019
Overview
Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large multisubunit transcription factor IIH (TFIIH). Here we report the cryo-EM structure of an NER intermediate containing TFIIH and the NER factor XPA. Compared to its transcription conformation, the TFIIH structure is rearranged such that its ATPase subunits XPB and XPD bind double- and single-stranded DNA, consistent with their translocase and helicase activities, respectively. XPA releases the inhibitory kinase module of TFIIH, displaces a ‘plug’ element from the DNA-binding pore in XPD, and together with the NER factor XPG stimulates XPD activity. Our results explain how TFIIH is switched from a transcription to a repair factor, and provide the basis for a mechanistic analysis of the NER pathway.
The NER machinery contains the multisubunit transcription factor IIH (TFIIH) that opens the DNA repair bubble, scans for the lesion, and coordinates excision of the damaged site. Here the authors resolve the cryo-electron microscopy structure of the human core TFIIH-XPA-DNA complex and provide insights into its activation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 101/58
/ 82/83
/ Animals
/ DNA
/ DNA-Binding Proteins - genetics
/ DNA-Binding Proteins - metabolism
/ Humanities and Social Sciences
/ Humans
/ Insecta
/ Kinases
/ Lesions
/ Nuclear Proteins - metabolism
/ Repair
/ Science
/ Transcription Factor TFIIH - metabolism
/ Transcription Factors - genetics
/ Transcription Factors - metabolism
/ Xeroderma Pigmentosum Group A Protein - genetics
/ Xeroderma Pigmentosum Group A Protein - metabolism
/ Xeroderma Pigmentosum Group D Protein - genetics
