Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release

Journal of Molecular Biology
Emily V WongEnrique M De La Cruz

Abstract

Dbp5, DDX19 in humans, is an essential DEAD-box protein involved in mRNA export, which has also been linked to other cellular processes, including rRNA export and translation. Dbp5 ATPase activity is regulated by several factors, including RNA, the nucleoporin proteins Nup159 and Gle1, and the endogenous small-molecule inositol hexakisphosphate (InsP6). To better understand how these factors modulate Dbp5 activity and how this modulation relates to in vivo RNA metabolism, a detailed characterization of the Dbp5 mechanochemical cycle in the presence of those regulators individually or together is necessary. In this study, we test the hypothesis that Nup159 controls the ADP-bound state of Dbp5. In addition, the contributions of Mg2+ to the kinetics and thermodynamics of ADP binding to Dbp5 were assessed. Using a solution based in vitro approach, Mg2+ was found to slow ADP and ATP release from Dbp5 and increased the overall ADP and ATP affinities, as observed with other NTPases. Furthermore, Nup159 did not accelerate ADP release, while Gle1 actually slowed ADP release independent of Mg2+. These findings are not consistent with Nup159 acting as a nucleotide exchange factor to promote ADP release and Dbp5 ATPase cycling. Instead, in...Continue Reading

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Citations

May 29, 2020·Proceedings of the National Academy of Sciences of the United States of America·Nandan G PanditEnrique M De La Cruz
Aug 28, 2019·ELife·Azra LariBen Montpetit
Mar 19, 2019·Annual Review of Biochemistry·Daniel H Lin, André Hoelz
Nov 19, 2020·Cellular and Molecular Life Sciences : CMLS·Arvind Arul Nambi Rajan, Ben Montpetit

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