The structure of the TFIIH p34 subunit reveals a von Willebrand factor A like fold.

Dominik R Schmitt, Jochen Kuper, Agnes Elias, Caroline Kisker

Journal: PloS one 2015;9(7):e102389

PMID: 25013903

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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.

Address: Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Wuerzburg, Wuerzburg, Germany.

DOI: 10.1371/journal.pone.0102389

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https://antibodies.cancer.gov/detail/CPTC-ERCC2-1

MeSH Terms: Amino Acid Sequence, Chaetomium, Crystallography, X-Ray, Escherichia coli, Fungal Proteins, Gene Expression, Humans, Models, Molecular, Molecular Sequence Data, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Protein Subunits, RNA Helicases, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transcription Factor TFIIH, von Willebrand Factor