4UZX

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

4UZX の概要

• エントリーDOI: 10.2210/pdb4uzx/pdb
• 関連するPDBエントリー: 4UZM 4UZW
• NMR情報: BMRB: 25214
• 分子名称: PROTEIN THO1 (1 entity in total)
• 機能のキーワード: rna binding protein, tho1
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7501.49

構造登録者

Jacobsen, J.O.B.,Allen, M.D.,Freund, S.M.V.,Bycroft, M. (登録日: 2014-09-09, 公開日: 2014-12-17, 最終更新日: 2024-05-15)

主引用文献

Jacobsen, J.O.B.,Allen, M.D.,Freund, S.M.V.,Bycroft, M.
High-Resolution NMR Structures of the Domains of Saccharomyces Cerevisiae Tho1.
Acta Crystallogr.,Sect.F, 72:500-, 2016

PubMed Abstract: 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.

PubMed: 27303905
DOI: 10.1107/S2053230X16007597

実験手法

SOLUTION NMR