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The Structure of the TFIIH p34 Subunit Reveals a Von Willebrand Factor A Like Fold

Please always quote using this URN: urn:nbn:de:bvb:20-opus-119471
  • 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 pointRNA 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.show moreshow less

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Metadaten
Author: Dominik R. Schmitt, Jochen Kuper, Agnes Elias, Caroline Kisker
URN:urn:nbn:de:bvb:20-opus-119471
Document Type:Journal article
Faculties:Fakultät für Biologie / Julius-von-Sachs-Institut für Biowissenschaften
Language:English
Parent Title (English):PLoS ONE
ISSN:1932-6203
Year of Completion:2014
Volume:9
Issue:7
Pagenumber:e102389
Source:PLoS ONE 9(7): e102389. doi:10.1371/journal.pone.0102389
DOI:https://doi.org/10.1371/journal.pone.0102389
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/25013903
Dewey Decimal Classification:6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 612 Humanphysiologie
Tag:crystal structure; electron density; iodides; molecular structure; protein domains; protein structure; protein-protein interactions; sequence motif analysis
Release Date:2015/11/09
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung