A mechanistic model of COR15 protein function in plant freezing tolerance: integration of structural and functional characteristics

Thalhammer, Anja; Hincha, Dirk K.

doi:10.4161/15592324.2014.977722

Cited by 41 publications

(30 citation statements)

References 11 publications

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“…62 However, folding of the COR15 proteins does not strictly follow either of these routes, but rather an ''initial crowding-induced folding 4 membrane binding 4 enhanced folding'' pathway. 63 The COR15 proteins partially fold into amphipathic a-helices during freezing. Only in this partially-folded conformation that can be induced by freezing in vivo or by osmolytes in vitro (referred to in the term ''crowding-induced folding''), are they able to interact with membranes.…”

Section: Discussionmentioning

confidence: 99%

Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana

Navarro‐Retamal

Bremer

Alzate‐Morales

et al. 2016

Phys. Chem. Chem. Phys.

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The LEA (late embryogenesis abundant) proteins COR15A and COR15B from Arabidopsis thaliana are intrinsically disordered under fully hydrated conditions, but obtain α-helical structure during dehydration, which is reversible upon rehydration. To understand this unusual structural transition, both proteins were investigated by circular dichroism (CD) and molecular dynamics (MD) approaches. MD simulations showed unfolding of the proteins in water, in agreement with CD data obtained with both HIS-tagged and untagged recombinant proteins. Mainly intramolecular hydrogen bonds (H-bonds) formed by the protein backbone were replaced by H-bonds with water molecules. As COR15 proteins function in vivo as protectants in leaves partially dehydrated by freezing, unfolding was further assessed under crowded conditions. Glycerol reduced (40%) or prevented (100%) unfolding during MD simulations, in agreement with CD spectroscopy results. H-bonding analysis indicated that preferential exclusion of glycerol from the protein backbone increased stability of the folded state.

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Section: Discussionmentioning

confidence: 99%

Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana

Navarro‐Retamal

Bremer

Alzate‐Morales

et al. 2016

Phys. Chem. Chem. Phys.

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“…A similar prediction pattern, combining high disorder probability with a high propensity for α-helix formation, has been reported for LEA proteins previously by Janis et al [40], who suggested that such a prediction pattern might indicate folding potential. We have previously shown that COR15A folds into amphipathic α-helices in response to reduced water availability [14,31], which drives membrane association and stabilization [32,41]. This structural element requires a regular distribution of hydrophobic amino acids along the protein sequence, usually every N+3 and/or N+4 positions, separated by polar residues [42].…”

Section: Bioinformatic Characterization Of the A Thaliana Lea_4 Familymentioning

confidence: 99%

Similar Yet Different–Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins

Knox-Brown

Rindfleisch

Günther

et al. 2020

IJMS

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The importance of intrinsically disordered late embryogenesis abundant (LEA) proteins in the tolerance to abiotic stresses involving cellular dehydration is undisputed. While structural transitions of LEA proteins in response to changes in water availability are commonly observed and several molecular functions have been suggested, a systematic, comprehensive and comparative study of possible underlying sequence-structure-function relationships is still lacking. We performed molecular dynamics (MD) simulations as well as spectroscopic and light scattering experiments to characterize six members of two distinct, lowly homologous clades of LEA_4 family proteins from Arabidopsis thaliana. We compared structural and functional characteristics to elucidate to what degree structure and function are encoded in LEA protein sequences and complemented these findings with physicochemical properties identified in a systematic bioinformatics study of the entire Arabidopsis thaliana LEA_4 family. Our results demonstrate that although the six experimentally characterized LEA_4 proteins have similar structural and functional characteristics, differences concerning their folding propensity and membrane stabilization capacity during a freeze/thaw cycle are obvious. These differences cannot be easily attributed to sequence conservation, simple physicochemical characteristics or the abundance of sequence motifs. Moreover, the folding propensity does not appear to be correlated with membrane stabilization capacity. Therefore, the refinement of LEA_4 structural and functional properties is likely encoded in specific patterns of their physicochemical characteristics.

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“…Among these genes, AtCor15 and AtCor78 are the most characterized. Reports have shown that AtCor15 is a chloroplast stromal protein that protects chloroplast membranes during freezing stress [ 14 , 15 , 16 ]. Further, AtCor78 , also known as AtRD29A (responsive to dehydration, RD), is involved in the response to cold, dehydration, and salt stressors [ 17 , 18 , 19 ].…”

Section: Introductionmentioning

confidence: 99%

PsCor413pm2, a Plasma Membrane-Localized, Cold-Regulated Protein from Phlox subulata, Confers Low Temperature Tolerance in Arabidopsis

Zhou

Liu

et al. 2018

IJMS

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Low temperature stress adversely affects plant growth and development. Isolation and characterization of cold response genes from cold-tolerant plants help to understand the mechanism underlying low temperature tolerance. In this study, PsCor413pm2, a cold-regulated (COR) gene isolated from Phlox subulata, was transferred to Arabidopsis plants to investigate its function. Real-time quantitative PCR analysis revealed that PsCor413pm2 expression was induced by cold. Subcellular localization revealed that the PsCor413pm2-green fluorescent protein (GFP) fusion protein localized to the plasma membrane in tobacco and Arabidopsis plants. Furthermore, overexpression of PsCor413pm2 in Arabidopsis plants enhanced tolerance to low temperature stress. Transgenic Arabidopsis roots had more influx of Ca2+ after a cold shock than wild-type plants, as shown using non-invasive micro-test technology (NMT). Moreover, the transcription abundance of five COR and two C-repeat (CRT) binding factor (CBF) genes in transgenic Arabidopsis plants was higher than that in the wild-type plants under cold stress. Taken together, our results suggest that overexpression of PsCor413pm2 enhances low temperature tolerance in Arabidopsis plants by affecting Ca2+ flux and the expression of stress-related COR and CBF genes.

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A mechanistic model of COR15 protein function in plant freezing tolerance: integration of structural and functional characteristics

Cited by 41 publications

References 11 publications

Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana

Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana

Similar Yet Different–Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins

PsCor413pm2, a Plasma Membrane-Localized, Cold-Regulated Protein from Phlox subulata, Confers Low Temperature Tolerance in Arabidopsis

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