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

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 endog...

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Published inJournal of molecular biology Vol. 430; no. 14; pp. 2080 - 2095
Main Authors Wong, Emily V., Gray, Shawn, Cao, Wenxiang, Montpetit, Rachel, Montpetit, Ben, De La Cruz, Enrique M.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 06.07.2018
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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 the presence of Nup159, the interaction between Gle1 and ADP-bound Dbp5 was found to be reduced by ~18-fold, suggesting that Nup159 alters the Dbp5–Gle1 interaction to aid Gle1 release from Dbp5. [Display omitted] •We test the hypothesis that Nup159 and Gle1 control the ADP-bound state of Dbp5.•We also assess the contributions of Mg2+ to the kinetics and thermodynamics of ADP binding to Dbp5.•Mg2+ slows mantADP and mantATP release from Dbp5 and increases the overall ADP and ATP affinities.•Nup159 does not accelerate mantADP or Mg2+–mantADP release, while Gle1/InsP6 slows mantADP release ~2-fold independent of Mg2+.•These findings are inconsistent with Nup159 or Gle1 acting as a NEF.
AbstractList 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 the presence of Nup159, the interaction between Gle1 and ADP-bound Dbp5 was found to be reduced by ~18-fold, suggesting that Nup159 alters the Dbp5-Gle1 interaction to aid Gle1 release from Dbp5.
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 the presence of Nup159, the interaction between Gle1 and ADP-bound Dbp5 was found to be reduced by ~18-fold, suggesting that Nup159 alters the Dbp5–Gle1 interaction to aid Gle1 release from Dbp5. [Display omitted] •We test the hypothesis that Nup159 and Gle1 control the ADP-bound state of Dbp5.•We also assess the contributions of Mg2+ to the kinetics and thermodynamics of ADP binding to Dbp5.•Mg2+ slows mantADP and mantATP release from Dbp5 and increases the overall ADP and ATP affinities.•Nup159 does not accelerate mantADP or Mg2+–mantADP release, while Gle1/InsP6 slows mantADP release ~2-fold independent of Mg2+.•These findings are inconsistent with Nup159 or Gle1 acting as a NEF.
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 (InsP 6 ). 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 Mg 2+ to the kinetics and thermodynamics of ADP binding to Dbp5 were assessed. Using a solution based in vitro approach, Mg 2+ was found to slow ADP and ATP release from Dbp5 and increased the overall ADP and ATP affinities, as observed with other NTPases. Further, Nup159 did not accelerate ADP release, while Gle1 actually slowed ADP release independent of Mg 2+ . These findings are not consistent with Nup159 acting as a nucleotide exchange factor to promote ADP release and Dbp5 ATPase cycling. Instead, in the presence of Nup159, the interaction between Gle1 and ADP-bound Dbp5 was found to be reduced by ~18-fold, suggesting that Nup159 alters the Dbp5-Gle1 interaction to aid Gle1 release from Dbp5.
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 (InsP ). 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 Mg to the kinetics and thermodynamics of ADP binding to Dbp5 were assessed. Using a solution based in vitro approach, Mg 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 Mg . These findings are not consistent with Nup159 acting as a nucleotide exchange factor to promote ADP release and Dbp5 ATPase cycling. Instead, in the presence of Nup159, the interaction between Gle1 and ADP-bound Dbp5 was found to be reduced by ~18-fold, suggesting that Nup159 alters the Dbp5-Gle1 interaction to aid Gle1 release from Dbp5.
Author Cao, Wenxiang
Gray, Shawn
Wong, Emily V.
Montpetit, Ben
Montpetit, Rachel
De La Cruz, Enrique M.
AuthorAffiliation a Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA
b Departments of Viticulture and Enology and Food Science and Technology, University of California, Davis, Davis, CA, USA
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Issue 14
Keywords Gle1
NEFs
Nup159
Dbp5
DBP
DEAD-box protein
kinetics
Language English
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Snippet 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...
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SubjectTerms Dbp5
DEAD-box protein
Gle1
kinetics
Nup159
Title Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release
URI https://dx.doi.org/10.1016/j.jmb.2018.05.025
https://www.ncbi.nlm.nih.gov/pubmed/29782832
https://search.proquest.com/docview/2042751449
https://pubmed.ncbi.nlm.nih.gov/PMC6003625
Volume 430
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