Sus1, Cdc31, and the Sac3 CID Region Form a Conserved Interaction Platform that Promotes Nuclear Pore Association and mRNA Export

被引：115

作者：

Jani, Divyang ^{[1
]}

Lutz, Sheila ^{[2
]}

Marshall, Neil J. ^{[1
]}

Fischer, Tamas ^{[2
]}

Koehler, Alwin ^{[2
]}

Ellisdon, Andrew M. ^{[1
]}

Hurt, Ed ^{[2
]}

Stewart, Murray ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Heidelberg Univ, Zentrum Biochem, INF328, D-69120 Heidelberg, Germany

来源：

MOLECULAR CELL | 2009年 / 33卷 / 06期

基金：

奥地利科学基金会;

关键词：

PROTEIN COMPLEX; BINDING SITES; GENE; TRANSCRIPTION; TREX; SAGA; RECRUITMENT; LOCALIZES; CENTRIN;

D O I：

10.1016/j.molcel.2009.01.033

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The yeast Sac3:Cdc31:Sus1:Thp1 (TREX-2) complex facilitates the repositioning and association of actively transcribing genes with nuclear pores (NPCs)-"gene gating"-that is central to integrating transcription, processing, and mRNA nuclear export. We present here the crystal structure of Sus1 and Cdc31 bound to a central region of Sac3 (the CID domain) that is crucial for its function. Sac3(CID) forms a long, gently undulating alpha helix around which one Cdc31 and two Sus1 chains are wrapped. Sus1 has an articulated helical hairpin fold that facilitates its wrapping around Sac3. In vivo studies using engineered mutations that selectively disrupted binding of individual chains to Sac3 indicated that Sus1 and Cdc31 function synergistically to promote NPC association of TREX-2 and mRNA nuclear export. These data indicate Sac3(CID) provides a scaffold within TREX-2 to integrate interactions between protein complexes to facilitate the coupling of transcription and mRNA export during gene expression.

引用

页码：727 / 737

页数：11

共 46 条

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