5aim
From Proteopedia
Crystal structure of T138 central eWH domain
Structural highlights
FunctionTFC3_YEAST TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. TFC3 is essential for cell viability. Cooperates with TFC6 in DNA binding.[1] [2] [3] Publication Abstract from PubMedIn eukaryotes, RNA Polymerase III (Pol III) is specifically responsible for transcribing genes encoding tRNAs and other short non-coding RNAs. The recruitment of Pol III to tRNA-encoding genes requires the transcription factors (TF) IIIB and IIIC. TFIIIC has been described as a conserved, multi-subunit protein complex composed of two subcomplexes, called tauA and tauB. How these two subcomplexes are linked and how their interaction affects the formation of the Pol III pre-initiation complex (PIC) is poorly understood. Here we use chemical crosslinking mass spectrometry and determine the molecular architecture of TFIIIC. We further report the crystal structure of the essential TPR array from tauA subunit tau131 and characterize its interaction with a central region of tauB subunit tau138. The identified tau131-tau138 interacting region is essential in vivo and overlaps with TFIIIB-binding sites, revealing a crucial interaction platform for the regulation of tRNA transcription initiation. Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.,Male G, von Appen A, Glatt S, Taylor NM, Cristovao M, Groetsch H, Beck M, Muller CW Nat Commun. 2015 Jun 10;6:7387. doi: 10.1038/ncomms8387. PMID:26060179[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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