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

AbstractRadical-Induced Cell Death1 (RCD1) functions as a cellular hub interacting with intrinsically disordered transcription factor regions, which lack a well-defined three-dimensional structure, to regulate plant stress. Here, we address the molecular evolution of the RCD1-interactome. Using bioinformatics, its history was traced back more than 480 million years to the emergence of land plants with the RCD1-binding short linear motif (SLiM) identified from mosses to flowering plants. SLiM variants were biophysically verified to be functional and to depend on the same RCD1 residues as the DREB2A transcription factor. Based on this, numerous additional members may be assigned to the RCD1-interactome. Conservation was further strengthened by similar intrinsic disorder profiles of the transcription factor homologs. The unique structural plasticity of the RCD1-interactome, with RCD1-binding induced α-helix formation in DREB2A, but not detectable in ANAC046 or ANAC013, is apparently conserved. Thermodynamic analysis also indicated conservation with interchangeability between Arabidopsis and soybean RCD1 and DREB2A, although with fine-tuned co-evolved binding interfaces. Interruption of conservation was observed, as moss DREB2 lacked the SLiM, likely reflecting differences in plant stress responses. This whole-interactome study uncovers principles of the evolution of SLiM:hub-interactions, such as conservation of α-helix propensities, which may be paradigmatic for disorder-based interactomes in eukaryotes.

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Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14

Cells ◽

10.3390/cells9081856 ◽

2020 ◽

Vol 9 (8) ◽

pp. 1856

Author(s):

Nikoletta Murvai ◽

Lajos Kalmar ◽

Bianka Szalaine Agoston ◽

Beata Szabo ◽

Agnes Tantos ◽

...

Keyword(s):

Heat Stress ◽

Intrinsically Disordered Proteins ◽

Stress Protein ◽

Structural Disorder ◽

Disordered Proteins ◽

Sequence Motifs ◽

E Coli ◽

Intrinsically Disordered

Details of the functional mechanisms of intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect the molecular mechanism of action of an IDP in cells by detailed structural analyses based on an in-cell nuclear magnetic resonance experiment. We show that the ID stress protein (IDSP) A. thaliana Early Response to Dehydration (ERD14) is capable of protecting E. coli cells under heat stress. The overexpression of ERD14 increases the viability of E. coli cells from 38.9% to 73.9% following heat stress (50 °C × 15 min). We also provide evidence that the protection is mainly achieved by protecting the proteome of the cells. In-cell NMR experiments performed in E. coli cells show that the protective activity is associated with a largely disordered structural state with conserved, short sequence motifs (K- and H-segments), which transiently sample helical conformations in vitro and engage in partner binding in vivo. Other regions of the protein, such as its S segment and its regions linking and flanking the binding motifs, remain unbound and disordered in the cell. Our data suggest that the cellular function of ERD14 is compatible with its residual structural disorder in vivo.

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Membrane-induced folding of the plant-stress protein Lti30.

PLANT PHYSIOLOGY ◽

10.1104/pp.15.01531 ◽

2016 ◽

pp. pp.01531.2015 ◽

Cited By ~ 8

Author(s):

Sylvia Eriksson ◽

Nadejda Eremina ◽

Andreas Barth ◽

Jens Danielsson ◽

Pia Harryson

Keyword(s):

Plant Stress ◽

Stress Protein ◽

Induced Folding

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

Biophysical Journal ◽

10.1016/j.bpj.2016.07.001 ◽

2016 ◽

Vol 111 (3) ◽

pp. 480-491 ◽

Cited By ~ 12

Author(s):

John Atkinson ◽

Matthew W. Clarke ◽

Josephine M. Warnica ◽

Kelly F. Boddington ◽

Steffen P. Graether

Keyword(s):

Membrane Surface ◽

Stress Protein ◽

Intrinsically Disordered

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CsrA-controlled proteins important for Acinetobacter baumannii desiccation tolerance

10.1101/2021.08.11.455981 ◽

2021 ◽

Author(s):

Yasuhiro Oda ◽

Madelyn M Shapiro ◽

Nathan M. Lewis ◽

Xuefei Zhong ◽

Holly K. Huse ◽

...

Keyword(s):

Amino Acid ◽

Acinetobacter Baumannii ◽

Desiccation Tolerance ◽

Protein A ◽

Stress Protein ◽

Intrinsically Disordered Protein ◽

Opportunistic Pathogen ◽

Nucleic Acid Binding ◽

Intrinsically Disordered ◽

Hospital Environments

Hospital environments serve as excellent reservoirs for the opportunistic pathogen Acinetobacter baumannii in part because it is exceptionally tolerant to desiccation. To understand the functional basis this trait, we used transposon sequencing (Tn-seq) to identify genes contributing to desiccation tolerance in A. baumannii strain AB5075. We identified 142 candidate desiccation tolerance genes, one of which encoded the global post-transcriptional regulator CsrA. We characterized CsrA in more detail by using proteomics to identify proteins that were differentially present in wild type and csrA mutant cells. Among these were a predicted universal stress protein A, an iron-containing redox protein, a KGG-domain containing protein, and catalase. Subsequent mutant analysis showed that each of these proteins was required for A. baumannii desiccation tolerance. The amino acid sequence of the KGG-domain containing protein predicts that it is an intrinsically disordered protein. Such proteins are critical for desiccation tolerance of the small animals called tardigrades. This protein also has a repeat nucleic acid binding amino acid motif, suggesting that it may protect A. baumannii DNA from desiccation-induced damage.

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