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. 2013 Sep 12;4:363.
doi: 10.3389/fpls.2013.00363.

Protein Intrinsic Disorder in Plants

Free PMC article

Protein Intrinsic Disorder in Plants

Florencio Pazos et al. Front Plant Sci. .
Free PMC article


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.

Keywords: biological networks; plant environmental responses; protein function; protein interactions; protein intrinsic disorder; protein structure.


Example of a highly disordered protein in A. thaliana. Schematic representation of the structural features of the “ putative NAC domain-containing protein 94” (Uniprot: NAC94_ARATH). The disorder prediction of IUPRED (Dosztanyi et al., 2005) show that, according with the standard 0.5 threshold, most of the C-terminal part of the protein (from 150 to 337) is probably unstructured (dotted lines). The N-terminal DNA binding domain is probably structured and, indeed, a structural model can be generated based on the structure of a homolog (PDB:4dul_B, 62% sequence identity; solid line). So probably this protein “ looks like” the representation above: a short structured DNA-binding domain followed by a long flexible disordered region, involved in the binding of different partners.

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