Protein intrinsic disorder in plants

Florencio Pazos,Natalia Pietrosemoli,Roberto Solano,Juan A García-Martín

doi:10.3389/fpls.2013.00363

Florencio Pazos, Natalia Pietrosemoli + Show 2 more

Open Access

https://doi.org/10.3389/fpls.2013.00363

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Abstract

To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions. Proteins completely or partially unstructured in their native (functional) form are involved in key cellular processes underlain by complex networks of protein interactions. The intrinsic conformational flexibility of these disordered proteins allows them to bind multiple partners in transient interactions of high specificity and low affinity. In concordance, in plants this type of proteins has been found in processes requiring these complex and versatile interaction networks. These include transcription factor networks, where disordered proteins act as integrators of different signals or link different transcription factor subnetworks due to their ability to interact (in many cases simultaneously) with different partners. Similarly, they also serve as signal integrators in signaling cascades, such as those related to response to external stimuli. Disordered proteins have also been found in plants in many stress-response processes, acting as protein chaperones or protecting other cellular components and structures. In plants, it is especially important to have complex and versatile networks able to quickly and efficiently respond to changing environmental conditions since these organisms cannot escape and have no other choice than adapting to them. Consequently, protein disorder can play an especially important role in plants, providing them with a fast mechanism to obtain complex, interconnected and versatile molecular networks.

Highlights

Protein intrinsic disorder in plantsDisordered proteins/regions are associated with key cellular processes such as signaling cascades, transcription regulation, cell cycle control and chaperone activity (Iakoucheva et al, 2002; Uversky et al, 2005; Tompa et al, 2006; Xie et al, 2007)
Reviewed by: Katja Baerenfaller, Swiss Federal Institute of Technology Zurich, Switzerland Sandra Karin Tanz, The University of Western Australia, Australia
To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions

Summary

Protein intrinsic disorder in plants

Disordered proteins/regions are associated with key cellular processes such as signaling cascades, transcription regulation, cell cycle control and chaperone activity (Iakoucheva et al, 2002; Uversky et al, 2005; Tompa et al, 2006; Xie et al, 2007) These processes require reversible transient interactions of high specificity www.frontiersin.org. Signaling networks are branched and interconnected, and they require transient interactions of high specificity with different partners, making unstructured proteins excellent candidates for them Another prototypical example are the molecular chaperones, for which a growing body of evidence points to the involvement of disorder in the activity of many of them (Kovacs and Tompa, 2012). It has been shown that in many cases alternative splicing isoforms are characterized by the addition/deletion of IDRs so as to add/remove interacting regions and tune the “wiring” of the networks these isoforms are involved in (Romero et al, 2006; Buljan et al, 2013)

PROTEIN DISORDER IN PLANTS

Findings

CONCLUSIONS