ArticlePloS one2014
The structure of the TFIIH p34 subunit reveals a von Willebrand factor A like fold.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Article
- The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH.Nucleic acids research · 2017Article
- Function of Conserved Topological Regions within the Saccharomyces cerevisiae Basal Transcription Factor TFIIH.Molecular and cellular biology · 2016Article
- Article
- Architecture of the Human and Yeast General Transcription and DNA Repair Factor TFIIH.Molecular cell · 2015Article
- Crystal structure of the Rad3/XPD regulatory domain of Ssl1/p44.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA polymerase II dependent transcription and nucleotide excision repair are mediated by a multifaceted interplay of subunits within the general transcription factor II H (TFIIH). A better understanding of the molecular structure of TFIIH is the key to unravel the mechanism of action of this versatile protein complex within these vital cellular processes. The importance of this complex becomes further evident in the context of severe diseases like xeroderma pigmentosum, Cockayne's syndrome and trichothiodystrophy, that arise from single point mutations in TFIIH subunits. Here we describe the structure of the p34 subunit of the TFIIH complex from the eukaryotic thermophilic fungus Chaetomium thermophilum. The structure revealed that p34 contains a von Willebrand Factor A (vWA) like domain, a fold which is generally known to be involved in protein-protein interactions. Within TFIIH p34 strongly interacts with p44, a positive regulator of the helicase XPD. Putative protein-protein interfaces are analyzed and possible binding sites for the p34-p44 interaction suggested.
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