Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2

eLife

Yi Ren¹  Yihu Xie¹  Austin L Ivey¹  Bradley P Clarke¹  Pate S Hill¹  Yi Shi²  Yong Joon Kim² 

[1] Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, United States;Department of Cell Biology, University of Pittsburgh, Pittsburgh, United States;Medical Scientist Training Program, University of Pittsburgh and Carnegie Mellon University, Pittsburgh, United States;

关键词: mRNA nuclear export;    DEAD-box ATPase;    SR protein;    mRNP remodeling;    S. cerevisiae;   

DOI  :  10.7554/eLife.65699

来源: eLife Sciences Publications, Ltd

【 摘 要 】

The evolutionarily conserved TRanscript-EXport (TREX) complex plays central roles during mRNP (messenger ribonucleoprotein) maturation and export from the nucleus to the cytoplasm. In yeast, TREX is composed of the THO sub-complex (Tho2, Hpr1, Tex1, Mft1, and Thp2), the DEAD box ATPase Sub2, and Yra1. Here we present a 3.7 Å cryo-EM structure of the yeast THO•Sub2 complex. The structure reveals the intimate assembly of THO revolving around its largest subunit Tho2. THO stabilizes a semi-open conformation of the Sub2 ATPase via interactions with Tho2. We show that THO interacts with the serine–arginine (SR)-like protein Gbp2 through both the RS domain and RRM domains of Gbp2. Cross-linking mass spectrometry analysis supports the extensive interactions between THO and Gbp2, further revealing that RRM domains of Gbp2 are in close proximity to the C-terminal domain of Tho2. We propose that THO serves as a landing pad to configure Gbp2 to facilitate its loading onto mRNP.

【 授权许可】

CC BY