Does water stress promote the proteome-wide adjustment of intrinsically disordered proteins in plants?

Does water stress promote the proteome-wide adjustment of intrinsically disordered proteins in... Plant response to water stress involves the activation of mechanisms expected to help them cope with water scarcity. Among these mechanisms, proteome-wide adjustment is well known. This includes actions to save energy, protect cellular and molecular components, and maintain vital functions of the cell. Intrinsically disordered proteins, which are proteins without a rigid three-dimensional structure, are seen as emerging multifunctional cellular components of proteomes. They are highly abundant in eukaryotic proteomes, and numerous functions for these proteins have been proposed. Here, we discuss several reasons why the collection of intrinsically disordered proteins in a proteome (disordome) could be subjected to an active regulation during conditions of water scarcity in plants. We also discuss the potential misinterpretations of disordome content estimations made so far due to bias-prone data and the need for reliable analysis based on experimental data in order to acknowledge the plasticity nature of the disordome. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cell Stress and Chaperones Springer Journals

Does water stress promote the proteome-wide adjustment of intrinsically disordered proteins in plants?

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Publisher
Springer Journals
Copyright
Copyright © 2018 by Cell Stress Society International
Subject
Biomedicine; Biomedicine, general; Cell Biology; Biochemistry, general; Immunology; Cancer Research; Neurosciences
ISSN
1355-8145
eISSN
1466-1268
D.O.I.
10.1007/s12192-018-0918-x
Publisher site
See Article on Publisher Site

Abstract

Plant response to water stress involves the activation of mechanisms expected to help them cope with water scarcity. Among these mechanisms, proteome-wide adjustment is well known. This includes actions to save energy, protect cellular and molecular components, and maintain vital functions of the cell. Intrinsically disordered proteins, which are proteins without a rigid three-dimensional structure, are seen as emerging multifunctional cellular components of proteomes. They are highly abundant in eukaryotic proteomes, and numerous functions for these proteins have been proposed. Here, we discuss several reasons why the collection of intrinsically disordered proteins in a proteome (disordome) could be subjected to an active regulation during conditions of water scarcity in plants. We also discuss the potential misinterpretations of disordome content estimations made so far due to bias-prone data and the need for reliable analysis based on experimental data in order to acknowledge the plasticity nature of the disordome.

Journal

Cell Stress and ChaperonesSpringer Journals

Published: Jun 2, 2018

References

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