Literature DB >> 28643166

Structural disorder in plant proteins: where plasticity meets sessility.

Alejandra A Covarrubias1, Cesar L Cuevas-Velazquez2, Paulette S Romero-Pérez2, David F Rendón-Luna2, Caspar C C Chater2.   

Abstract

Plants are sessile organisms. This intriguing nature provokes the question of how they survive despite the continual perturbations caused by their constantly changing environment. The large amount of knowledge accumulated to date demonstrates the fascinating dynamic and plastic mechanisms, which underpin the diverse strategies selected in plants in response to the fluctuating environment. This phenotypic plasticity requires an efficient integration of external cues to their growth and developmental programs that can only be achieved through the dynamic and interactive coordination of various signaling networks. Given the versatility of intrinsic structural disorder within proteins, this feature appears as one of the leading characters of such complex functional circuits, critical for plant adaptation and survival in their wild habitats. In this review, we present information of those intrinsically disordered proteins (IDPs) from plants for which their high level of predicted structural disorder has been correlated with a particular function, or where there is experimental evidence linking this structural feature with its protein function. Using examples of plant IDPs involved in the control of cell cycle, metabolism, hormonal signaling and regulation of gene expression, development and responses to stress, we demonstrate the critical importance of IDPs throughout the life of the plant.

Entities:  

Keywords:  Intrinsically disordered proteins; LEA proteins; Plant development; Plant metabolism; Plant signaling; Plant stress responses; Transcription factors

Mesh:

Substances:

Year:  2017        PMID: 28643166     DOI: 10.1007/s00018-017-2557-2

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  274 in total

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3.  Phosphorylation of MAP65-1 by Arabidopsis Aurora Kinases Is Required for Efficient Cell Cycle Progression.

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Journal:  Plant Physiol       Date:  2016-11-22       Impact factor: 8.340

Review 4.  The Phage Shock Protein Response.

Authors:  Josué Flores-Kim; Andrew J Darwin
Journal:  Annu Rev Microbiol       Date:  2016-06-08       Impact factor: 15.500

5.  Proteins as molecular chaperones.

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Journal:  Nature       Date:  1987 Jul 30-Aug 5       Impact factor: 49.962

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Journal:  Mol Plant       Date:  2015-03-17       Impact factor: 13.164

7.  Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins.

Authors:  Denes Kovacs; Eva Kalmar; Zsolt Torok; Peter Tompa
Journal:  Plant Physiol       Date:  2008-03-21       Impact factor: 8.340

8.  The bacterial-type phosphoenolpyruvate carboxylase isozyme from developing castor oil seeds is subject to in vivo regulatory phosphorylation at serine-451.

Authors:  Katie J Dalziel; Brendan O'Leary; Carolyne Brikis; Srinath K Rao; Yi-Min She; Terry Cyr; William C Plaxton
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9.  P(3)DB: An Integrated Database for Plant Protein Phosphorylation.

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Journal:  Plant Signal Behav       Date:  2012-11-15
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  17 in total

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Authors:  Martin Balcerowicz
Journal:  Plant Physiol       Date:  2020-06       Impact factor: 8.340

2.  An Intrinsically Disordered Protein Interacts with the Cytoskeleton for Adaptive Root Growth under Stress.

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Journal:  Plant Physiol       Date:  2020-04-01       Impact factor: 8.340

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Journal:  Nat Commun       Date:  2020-05-08       Impact factor: 14.919

7.  Evolution of Protein Ductility in Duplicated Genes of Plants.

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Journal:  Front Plant Sci       Date:  2018-08-20       Impact factor: 5.753

8.  Determining the Protective Activity of IDPs Under Partial Dehydration and Freeze-Thaw Conditions.

Authors:  David F Rendón-Luna; Paulette S Romero-Pérez; Cesar L Cuevas-Velazquez; José L Reyes; Alejandra A Covarrubias
Journal:  Methods Mol Biol       Date:  2020

9.  Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14.

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10.  Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii.

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Journal:  Sci Rep       Date:  2018-05-01       Impact factor: 4.379

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