eLife | |
Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2 | |
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
【 预 览 】
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