Global Dynamics in Protein Disorder during Maize Seed Development.

Zamora-Briseño Zamora-Briseño,Rodríguez-Zapata Rodríguez-Zapata,Reyes-Hernández Reyes-Hernández,Castaño Castaño,Pereira-Santana Pereira-Santana

doi:10.3390/genes10070502

Abstract

Intrinsic protein disorder is a physicochemical attribute of some proteins lacking tridimensional structure and is collectively known as intrinsically disordered proteins (IDPs). Interestingly, several IDPs have been associated with protective functions in plants and with their response to external stimuli. To correlate the modulation of the IDPs content with the developmental progression in seed, we describe the expression of transcripts according to the disorder content of the proteins that they codify during seed development, from the early embryogenesis to the beginning of the desiccation tolerance acquisition stage. We found that the total expression profile of transcripts encoding for structured proteins is highly increased during middle phase. However, the relative content of protein disorder is increased as seed development progresses. We identified several intrinsically disordered transcription factors that seem to play important roles throughout seed development. On the other hand, we detected a gene cluster encoding for IDPs at the end of the late phase, which coincides with the beginning of the acquisition of desiccation tolerance. In conclusion, the expression pattern of IDPs is highly dependent on the developmental stage, and there is a general reduction in the expression of transcripts encoding for structured proteins as seed development progresses. We proposed maize seeds as a model to study the regulation of protein disorder in plant development and its involvement in the acquisition of desiccation tolerance in plants.

Highlights

Over the last few years, new information has been generated regarding the role of intrinsically disordered proteins (IDPs) which has changed our understanding of protein biochemistry
We found a clear relationship in the protein length and the protein disorder content (Figure 1)
Disordered proteins are enriched in regulatory function, in contrast to structured proteins which are enriched in catalytic functions (Figure 2A)

Summary

Introduction

Over the last few years, new information has been generated regarding the role of intrinsically disordered proteins (IDPs) which has changed our understanding of protein biochemistry. IDPs possess low complexity and a biased composition of amino acid (aa), being almost depleted in hydrophobic and aromatic residues while enriched in polar and charged aa [1]. These features in the primary structure confer them with a high net charge and low mean hydrophobicity [2]. For these reasons, such protein sequences are unable to fold into stable, rigid, globular, three-dimensional structures. Some proteins are predicted to be entirely disordered (IDPs in sensu stricto), while others are not intrinsically disordered throughout, but have disordered segments

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Conclusion