IDPs (intrinsically disordered proteins) are highly abundant in eukaryotic proteomes and important for cellular functions, especially in cell signalling and transcriptional regulation. An IDR (intrinsically disordered region) within an IDP often undergoes disorder-to-order transitions upon binding to various partners, allowing an IDP to recognize and bind different partners at various binding interfaces. Plant-specific GRAS proteins play critical and diverse roles in plant development and signalling, and act as integrators of signals from multiple plant growth regulatory and environmental inputs. Possessing an intrinsically disordered N-terminal domain, the GRAS proteins constitute the first functionally required unfoldome from the plant kingdom. Furthermore, the N-terminal domains of GRAS proteins contain MoRFs (molecular recognition features), short interaction-prone segments that are located within IDRs and are able to recognize their interacting partners by undergoing disorder-to-order transitions upon binding to these specific partners. These MoRFs represent potential protein–protein binding sites and may be acting as molecular bait in recognition events during plant development. Intrinsic disorder provides GRAS proteins with a degree of binding plasticity that may be linked to their functional versatility. As an overview of structure–function relationships for GRAS proteins, the present review covers the main biological functions of the GRAS family, the IDRs within these proteins and their implications for understanding mode-of-action.
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February 2012
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Review Article|
January 27 2012
GRAS proteins: the versatile roles of intrinsically disordered proteins in plant signalling
Xiaolin Sun;
Xiaolin Sun
1
*The New Zealand Institute for Plant and Food Research, Private Bag 11030, Palmerston North 4474, New Zealand
1To whom correspondence should be addressed (email xiaolin.sun@plantandfood.co.nz).
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William T. Jones;
William T. Jones
*The New Zealand Institute for Plant and Food Research, Private Bag 11030, Palmerston North 4474, New Zealand
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Erik H. A. Rikkerink
Erik H. A. Rikkerink
†The New Zealand Institute for Plant and Food Research, Private Bag 92169, Auckland 1041, New Zealand
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Publisher: Portland Press Ltd
Received:
October 03 2011
Revision Received:
October 28 2011
Accepted:
November 03 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 442 (1): 1–12.
Article history
Received:
October 03 2011
Revision Received:
October 28 2011
Accepted:
November 03 2011
Citation
Xiaolin Sun, William T. Jones, Erik H. A. Rikkerink; GRAS proteins: the versatile roles of intrinsically disordered proteins in plant signalling. Biochem J 15 February 2012; 442 (1): 1–12. doi: https://doi.org/10.1042/BJ20111766
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