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Title: High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1

In this study, high-resolution structures of both the N-terminal DNA-binding SAP domain and the C-terminal RNA-binding domain of S. cerevisiae Tho1 have been determined. THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. THO is thought to be formed from five subunits, Tho2p, Hpr1p, Tex1p, Mft1p and Thp2p, and recent work has determined a low-resolution structure of the complex [Poulsen et al. (2014 ▸), PLoS One, 9, e103470]. A number of additional proteins are thought to be involved in the formation of mRNP in yeast, including Tho1, which has been shown to bind RNA in vitro and is recruited to actively transcribed chromatin in vivo in a THO-complex and RNA-dependent manner. Tho1 is known to contain a SAP domain at the N-terminus, but the ability to suppress the expression defects of the hpr1Δ mutant of THO was shown to reside in the RNA-binding C-terminal region. In this study, high-resolution structures of both the N-terminal DNA-binding SAP domain and C-terminal RNA-binding domain have been determined.
Authors:
; ; ;  [1]
  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH (United Kingdom)
Publication Date:
OSTI Identifier:
22515187
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F, Structural Biology Communications; Journal Volume: 72; Journal Issue: Pt 6; Other Information: PMCID: PMC4909252; PMID: 27303905; PUBLISHER-ID: pq5029; PUBLISHER-ID: S2053230X16007597; OAI: oai:pubmedcentral.nih.gov:4909252; Copyright (c) Jacobsen et al. 2016; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CHROMATIN; COMPLEXES; COUPLING; DEFECTS; DNA; EXPORTS; IN VITRO; IN VIVO; MESSENGER-RNA; MUTANTS; NUCLEAR MAGNETIC RESONANCE; PARTICLES; PROCESSING; PROTEINS; RESOLUTION; SACCHAROMYCES CEREVISIAE; TRANSCRIPTION