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Structural polymorphism in the N-terminal oligomerization domain of NPM1.

Nucleophosmin (NPM1) is a multifunctional phospho-protein with critical roles in ribosome biogenesis, tumor suppression, and nucleolar stress response. Here we show that the N-terminal oligomerization domain of NPM1 (Npm-N) exhibits structural polymorphism by populating conformational states ranging... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America March 25, 2014, Vol.111(12), pp.4466-4471
Main Author: Mitrea, Diana M
Other Authors: Grace, Christy R , Buljan, Marija , Yun, Mi-Kyung , Pytel, Nicholas J , Satumba, John , Nourse, Amanda , Park, Cheon-Gil , Madan Babu, M , White, Stephen W , Kriwacki, Richard W
Format: Electronic Article Electronic Article
Language: English
Subjects:
NMR
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1321007111
Link: http://search.proquest.com/docview/1514435135/?pq-origsite=primo
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recordid: proquest1514435135
title: Structural polymorphism in the N-terminal oligomerization domain of NPM1.
format: Article
creator:
  • Mitrea, Diana M
  • Grace, Christy R
  • Buljan, Marija
  • Yun, Mi-Kyung
  • Pytel, Nicholas J
  • Satumba, John
  • Nourse, Amanda
  • Park, Cheon-Gil
  • Madan Babu, M
  • White, Stephen W
  • Kriwacki, Richard W
subjects:
  • Amino Acid Sequence–Chemistry
  • Biopolymers–Metabolism
  • Chromatography, Gel–Chemistry
  • Humans–Metabolism
  • Models, Molecular–Metabolism
  • Molecular Sequence Data–Metabolism
  • Native Polyacrylamide Gel Electrophoresis–Metabolism
  • Nuclear Magnetic Resonance, Biomolecular–Metabolism
  • Nuclear Proteins–Metabolism
  • Phosphorylation–Metabolism
  • Protein Binding–Metabolism
  • Protein Conformation–Metabolism
  • Biopolymers
  • Nuclear Proteins
  • Nucleophosmin
  • NMR
  • X-Ray Crystallography
ispartof: Proceedings of the National Academy of Sciences of the United States of America, March 25, 2014, Vol.111(12), pp.4466-4471
description: Nucleophosmin (NPM1) is a multifunctional phospho-protein with critical roles in ribosome biogenesis, tumor suppression, and nucleolar stress response. Here we show that the N-terminal oligomerization domain of NPM1 (Npm-N) exhibits structural polymorphism by populating conformational states ranging from a highly ordered, folded pentamer to a highly disordered monomer. The monomerpentamer equilibrium is modulated by posttranslational modification and protein binding. Phosphorylation drives the equilibrium in favor of monomeric forms, and this effect can be reversed by Npm-N binding to its interaction partners. We have identified a short, arginine-rich linear motif in NPM1 binding partners that mediates Npm-N oligomerization. We propose that the diverse functional repertoire associated with NPM1 is controlled through a regulated unfolding mechanism signaled through posttranslational modifications and intermolecular interactions. NMR | X-ray crystallography www.pnas.org/cgi/doi/10.1073/pnas.1321007111
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1321007111
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleStructural polymorphism in the N-terminal oligomerization domain of NPM1.
creatorMitrea, Diana M ; Grace, Christy R ; Buljan, Marija ; Yun, Mi-Kyung ; Pytel, Nicholas J ; Satumba, John ; Nourse, Amanda ; Park, Cheon-Gil ; Madan Babu, M ; White, Stephen W ; Kriwacki, Richard W
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identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1321007111
subjectAmino Acid Sequence–Chemistry ; Biopolymers–Metabolism ; Chromatography, Gel–Chemistry ; Humans–Metabolism ; Models, Molecular–Metabolism ; Molecular Sequence Data–Metabolism ; Native Polyacrylamide Gel Electrophoresis–Metabolism ; Nuclear Magnetic Resonance, Biomolecular–Metabolism ; Nuclear Proteins–Metabolism ; Phosphorylation–Metabolism ; Protein Binding–Metabolism ; Protein Conformation–Metabolism ; Biopolymers ; Nuclear Proteins ; Nucleophosmin ; NMR ; X-Ray Crystallography
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descriptionNucleophosmin (NPM1) is a multifunctional phospho-protein with critical roles in ribosome biogenesis, tumor suppression, and nucleolar stress response. Here we show that the N-terminal oligomerization domain of NPM1 (Npm-N) exhibits structural polymorphism by populating conformational states ranging from a highly ordered, folded pentamer to a highly disordered monomer. The monomerpentamer equilibrium is modulated by posttranslational modification and protein binding. Phosphorylation drives the equilibrium in favor of monomeric forms, and this effect can be reversed by Npm-N binding to its interaction partners. We have identified a short, arginine-rich linear motif in NPM1 binding partners that mediates Npm-N oligomerization. We propose that the diverse functional repertoire associated with NPM1 is controlled through a regulated unfolding mechanism signaled through posttranslational modifications and intermolecular interactions. NMR | X-ray crystallography www.pnas.org/cgi/doi/10.1073/pnas.1321007111
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authorMitrea, Diana M ; Grace, Christy R ; Buljan, Marija ; Yun, Mi-Kyung ; Pytel, Nicholas J ; Satumba, John ; Nourse, Amanda ; Park, Cheon-Gil ; Madan Babu, M ; White, Stephen W ; Kriwacki, Richard W
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