NDLI: Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding

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Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding

Content Provider	Scilit
Author	Banerjee, Priya R. Mitrea, Diana M. Kriwacki, Richard W. Deniz, Ashok A.
Copyright Year	2015
Description	Journal: Angewandte Chemie International Edition As for many intrinsically disordered proteins, order-disorder transitions in the N-terminal oligomerization domain of the multifunctional nucleolar protein nucleophosmin (Npm-N) are central to its function, with phosphorylation and partner binding acting as regulatory switches. However, the mechanism of this transition and its regulation remain poorly understood. In this study, single-molecule and ensemble experiments revealed pathways with alternative sequences of folding and assembly steps for Npm-N. Pathways could be switched by altering the ionic strength. Phosphorylation resulted in pathway-specific effects, and decoupled folding and assembly steps to facilitate disorder. Conversely, binding to a physiological partner locked Npm-N in ordered pentamers and counteracted the effects of phosphorylation. The mechanistic plasticity found in the Npm-N order-disorder transition enabled a complex interplay of phosphorylation and partner-binding steps to modulate its folding landscape.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4752826/pdf
Ending Page	1679
Page Count	5
Starting Page	1675
ISSN	14337851
e-ISSN	15213773
DOI	10.1002/anie.201507728
Journal	Angewandte Chemie International Edition
Issue Number	5
Volume Number	55
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2015-12-17
Access Restriction	Open
Subject Keyword	Journal: Angewandte Chemie International Edition Cell Biology Conformational Landscape Coupled Folding and Binding Protein Folding Single-molecule Fret
Content Type	Text
Resource Type	Article
Subject	Chemistry Catalysis

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