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Title: Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1

Abstract

mRNA is cotranscrptionally processed and packaged into messenger ribonucleoprotein particles (mRNPs) in the nucleus. Prior to export through the nuclear pore, mRNPs undergo several obligatory remodeling reactions. In yeast, one of these reactions involves loading of the mRNA-binding protein Yra1 by the DEAD-box ATPase Sub2 as assisted by the hetero-pentameric THO complex. To obtain molecular insights into reaction mechanisms, we determined crystal structures of two relevant complexes: a THO hetero-pentamer bound to Sub2 at 6.0 Å resolution; and Sub2 associated with an ATP analogue, RNA, and a C-terminal fragment of Yra1 (Yra1-C) at 2.6 Å resolution. We found that the 25 nm long THO clamps Sub2 in a half-open configuration; in contrast, when bound to the ATP analogue, RNA and Yra1-C, Sub2 assumes a closed conformation. Both THO and Yra1-C stimulated Sub2’s intrinsic ATPase activity. We propose that THO surveys common landmarks in each nuclear mRNP to localize Sub2 for targeted loading of Yra1.

Authors:
 [1];  [1]; ORCiD logo [1]
  1. Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, United States
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
HHMI
OSTI Identifier:
1430337
Resource Type:
Journal Article
Resource Relation:
Journal Name: eLife; Journal Volume: 6; Journal Issue: 2017
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Ren, Yi, Schmiege, Philip, and Blobel, Günter. Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1. United States: N. p., 2017. Web. doi:10.7554/eLife.20070.
Ren, Yi, Schmiege, Philip, & Blobel, Günter. Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1. United States. doi:10.7554/eLife.20070.
Ren, Yi, Schmiege, Philip, and Blobel, Günter. Fri . "Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1". United States. doi:10.7554/eLife.20070.
@article{osti_1430337,
title = {Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1},
author = {Ren, Yi and Schmiege, Philip and Blobel, Günter},
abstractNote = {mRNA is cotranscrptionally processed and packaged into messenger ribonucleoprotein particles (mRNPs) in the nucleus. Prior to export through the nuclear pore, mRNPs undergo several obligatory remodeling reactions. In yeast, one of these reactions involves loading of the mRNA-binding protein Yra1 by the DEAD-box ATPase Sub2 as assisted by the hetero-pentameric THO complex. To obtain molecular insights into reaction mechanisms, we determined crystal structures of two relevant complexes: a THO hetero-pentamer bound to Sub2 at 6.0 Å resolution; and Sub2 associated with an ATP analogue, RNA, and a C-terminal fragment of Yra1 (Yra1-C) at 2.6 Å resolution. We found that the 25 nm long THO clamps Sub2 in a half-open configuration; in contrast, when bound to the ATP analogue, RNA and Yra1-C, Sub2 assumes a closed conformation. Both THO and Yra1-C stimulated Sub2’s intrinsic ATPase activity. We propose that THO surveys common landmarks in each nuclear mRNP to localize Sub2 for targeted loading of Yra1.},
doi = {10.7554/eLife.20070},
journal = {eLife},
number = 2017,
volume = 6,
place = {United States},
year = {Fri Jan 06 00:00:00 EST 2017},
month = {Fri Jan 06 00:00:00 EST 2017}
}