The Structure of the TFIIH p34 Subunit Reveals a Von Willebrand Factor A Like Fold
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- 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.…
Autor(en): | Dominik R. Schmitt, Jochen Kuper, Agnes Elias, Caroline Kisker |
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URN: | urn:nbn:de:bvb:20-opus-119471 |
Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
Institute der Universität: | Fakultät für Biologie / Julius-von-Sachs-Institut für Biowissenschaften |
Sprache der Veröffentlichung: | Englisch |
Titel des übergeordneten Werkes / der Zeitschrift (Englisch): | PLoS ONE |
ISSN: | 1932-6203 |
Erscheinungsjahr: | 2014 |
Band / Jahrgang: | 9 |
Heft / Ausgabe: | 7 |
Seitenangabe: | e102389 |
Originalveröffentlichung / Quelle: | 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 |
Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 612 Humanphysiologie |
Freie Schlagwort(e): | crystal structure; electron density; iodides; molecular structure; protein domains; protein structure; protein-protein interactions; sequence motif analysis |
Datum der Freischaltung: | 09.11.2015 |
Lizenz (Deutsch): | CC BY: Creative-Commons-Lizenz: Namensnennung |