Literature DB >> 23362206

Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology.

Xiaolin Sun1, Erik H A Rikkerink, William T Jones, Vladimir N Uversky.   

Abstract

Intrinsically disordered proteins (IDPs) are highly abundant in eukaryotic proteomes. Plant IDPs play critical roles in plant biology and often act as integrators of signals from multiple plant regulatory and environmental inputs. Binding promiscuity and plasticity allow IDPs to interact with multiple partners in protein interaction networks and provide important functional advantages in molecular recognition through transient protein-protein interactions. Short interaction-prone segments within IDPs, termed molecular recognition features, represent potential binding sites that can undergo disorder-to-order transition upon binding to their partners. In this review, we summarize the evidence for the importance of IDPs in plant biology and evaluate the functions associated with intrinsic disorder in five different types of plant protein families experimentally confirmed as IDPs. Functional studies of these proteins illustrate the broad impact of disorder on many areas of plant biology, including abiotic stress, transcriptional regulation, light perception, and development. Based on the roles of disorder in the protein-protein interactions, we propose various modes of action for plant IDPs that may provide insight for future experimental approaches aimed at understanding the molecular basis of protein function within important plant pathways.

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Year:  2013        PMID: 23362206      PMCID: PMC3584547          DOI: 10.1105/tpc.112.106062

Source DB:  PubMed          Journal:  Plant Cell        ISSN: 1040-4651            Impact factor:   11.277


  124 in total

1.  Direct interaction of Arabidopsis cryptochromes with COP1 in light control development.

Authors:  H Wang; L G Ma; J M Li; H Y Zhao; X W Deng
Journal:  Science       Date:  2001-08-16       Impact factor: 47.728

2.  Preformed structural elements feature in partner recognition by intrinsically unstructured proteins.

Authors:  Monika Fuxreiter; István Simon; Peter Friedrich; Peter Tompa
Journal:  J Mol Biol       Date:  2004-05-14       Impact factor: 5.469

3.  N-terminal segments modulate the α-helical propensities of the intrinsically disordered basic regions of bZIP proteins.

Authors:  Rahul K Das; Scott L Crick; Rohit V Pappu
Journal:  J Mol Biol       Date:  2011-12-28       Impact factor: 5.469

4.  Phosphorylation of Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 facilitates cation-induced conformational changes and actin assembly.

Authors:  Luna N Rahman; Graham S T Smith; Vladimir V Bamm; Janine A M Voyer-Grant; Barbara A Moffatt; John R Dutcher; George Harauz
Journal:  Biochemistry       Date:  2011-10-10       Impact factor: 3.162

Review 5.  Intrinsically disordered chaperones in plants and animals.

Authors:  Peter Tompa; Denes Kovacs
Journal:  Biochem Cell Biol       Date:  2010-04       Impact factor: 3.626

6.  Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos.

Authors:  K M Campbell; A R Terrell; P J Laybourn; K J Lumb
Journal:  Biochemistry       Date:  2000-03-14       Impact factor: 3.162

7.  Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA.

Authors:  L M Podust; A M Krezel; Y Kim
Journal:  J Biol Chem       Date:  2001-01-05       Impact factor: 5.157

8.  Cold activation of a plasma membrane-tethered NAC transcription factor induces a pathogen resistance response in Arabidopsis.

Authors:  Pil Joon Seo; Mi Jung Kim; Ju-Young Park; Sun-Young Kim; Jin Jeon; Yong-Hwan Lee; Jungmook Kim; Chung-Mo Park
Journal:  Plant J       Date:  2009-11-26       Impact factor: 6.417

9.  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

10.  SLiMFinder: a web server to find novel, significantly over-represented, short protein motifs.

Authors:  Norman E Davey; Niall J Haslam; Denis C Shields; Richard J Edwards
Journal:  Nucleic Acids Res       Date:  2010-05-23       Impact factor: 16.971

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  66 in total

1.  Pipeline to Identify Hydroxyproline-Rich Glycoproteins.

Authors:  Kim L Johnson; Andrew M Cassin; Andrew Lonsdale; Antony Bacic; Monika S Doblin; Carolyn J Schultz
Journal:  Plant Physiol       Date:  2017-04-26       Impact factor: 8.340

Review 2.  Structural disorder in plant proteins: where plasticity meets sessility.

Authors:  Alejandra A Covarrubias; Cesar L Cuevas-Velazquez; Paulette S Romero-Pérez; David F Rendón-Luna; Caspar C C Chater
Journal:  Cell Mol Life Sci       Date:  2017-06-22       Impact factor: 9.261

3.  Does water stress promote the proteome-wide adjustment of intrinsically disordered proteins in plants?

Authors:  Jesús Alejandro Zamora-Briseño; Sandi Julissa Reyes-Hernández; Luis Carlos Rodríguez Zapata
Journal:  Cell Stress Chaperones       Date:  2018-06-02       Impact factor: 3.667

4.  Effect of an Intrinsically Disordered Plant Stress Protein on the Properties of Water.

Authors:  Luisa A Ferreira; Alicyia Walczyk Mooradally; Boris Zaslavsky; Vladimir N Uversky; Steffen P Graether
Journal:  Biophys J       Date:  2018-09-22       Impact factor: 4.033

5.  A LEA 4 protein up-regulated by ABA is involved in drought response in maize roots.

Authors:  Jesús Alejandro Zamora-Briseño; Estela Sánchez de Jiménez
Journal:  Mol Biol Rep       Date:  2016-02-27       Impact factor: 2.316

6.  Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro.

Authors:  Nghiem X Dang; Antoneta V Popova; Michaela Hundertmark; Dirk K Hincha
Journal:  Planta       Date:  2014-05-20       Impact factor: 4.116

7.  A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties.

Authors:  Lucero Y Rivera-Najera; Gloria Saab-Rincón; Marina Battaglia; Carlos Amero; Nancy O Pulido; Enrique García-Hernández; Rosa M Solórzano; José L Reyes; Alejandra A Covarrubias
Journal:  J Biol Chem       Date:  2014-09-30       Impact factor: 5.157

8.  The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit.

Authors:  Cesar L Cuevas-Velazquez; Gloria Saab-Rincón; José Luis Reyes; Alejandra A Covarrubias
Journal:  J Biol Chem       Date:  2016-03-22       Impact factor: 5.157

9.  Structure of an Intrinsically Disordered Stress Protein Alone and Bound to a Membrane Surface.

Authors:  John Atkinson; Matthew W Clarke; Josephine M Warnica; Kelly F Boddington; Steffen P Graether
Journal:  Biophys J       Date:  2016-08-09       Impact factor: 4.033

10.  SmLEA2, a gene for late embryogenesis abundant protein isolated from Salvia miltiorrhiza, confers tolerance to drought and salt stress in Escherichia coli and S. miltiorrhiza.

Authors:  Huaiqin Wang; Yucui Wu; Xinbing Yang; Xiaorong Guo; Xiaoyan Cao
Journal:  Protoplasma       Date:  2016-05-18       Impact factor: 3.356

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