Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity – an X-ray and light scattering study

Shou, Keyun; Bremer, Anne; Rindfleisch, Tobias; Knox-Brown, Patrick; Hirai, Mitsuhiro; Rekas, Agata; Garvey, Christopher J.; Hincha, Dirk K.; Stadler, Andreas M.; Thalhammer, Anja

doi:10.1039/c9cp01768b

Cited by 18 publications

(27 citation statements)

References 60 publications

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“…To obtain a representation of the natively folded state of the chosen proteins, we used 500 ns molecular dynamics (MD) simulations to equilibrate these models in 100% glycerol (Figure 9), comparable to our earlier reports on COR15A [31]. The simulation approach was suitable for five out of the six proteins due to their relatively small The datasets for COR15A in the presence of all three solutes and for LEA11 and LEA25 in glycerol and TFE have been published previously [30,33]. Insets show the variance in negative ellipticity at 222 nm of the two LEA_4 clades.…”

Section: Structural Characterization Of the Two Lea_4 Clades By MD Simentioning

confidence: 85%

“…This was not true for the remaining LEA proteins. COR15A oligomerizes in response to high glycerol concentrations [33]. Whether such oligomerization also occurs for LEA25 and whether this is related to the increased folding, which is actually higher than the maximum folding potential of the monomers in TFE, remains to be determined.…”

Section: Discussionmentioning

confidence: 97%

“…Finally, LEA25 is localized in the cytoplasm and the corresponding gene is expressed in seeds and in vegetative tissues in response to high salt concentrations. We have previously described structural and functional details of four of the six proteins (COR15A, LEA7, LEA11, LEA25) [14,19,30,31,[33][34][35]39,44], but a comprehensive comparative analysis has not been provided.…”

Section: Experimental Structural Characterization Of the Members Of Tmentioning

confidence: 99%

“…Sci. 2020, 21, x FOR PEER REVIEW 7 of 26 LEA11, LEA25) [14,19,30,31,[33][34][35]39,44], but a comprehensive comparative analysis has not been provided.…”

Section: Experimental Structural Characterization Of the Members Of Tmentioning

confidence: 99%

“…We have contributed several studies on the LEA_4 proteins COR15A, COR15B, LEA25 and LEA11, all stemming from the same homology clade [19,[30][31][32][33]. All are essentially IDPs in the fully hydrated state, show a coil-helix transition in response to desiccation and partial dehydration and stabilize liposomes modeling the lipid composition of inner chloroplast membranes during a freeze/thaw cycle.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Structural Characterization Of the Two Lea_4 Clades By MD Simentioning

confidence: 85%

Section: Discussionmentioning

confidence: 97%

Section: Experimental Structural Characterization Of the Members Of Tmentioning

confidence: 99%

“…Sci. 2020, 21, x FOR PEER REVIEW 7 of 26 LEA11, LEA25) [14,19,30,31,[33][34][35]39,44], but a comprehensive comparative analysis has not been provided.…”

Section: Experimental Structural Characterization Of the Members Of Tmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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Helicity of a tardigrade disordered protein contributes to its protective function during desiccation

Biswas,

Gollub,

et al. 2024

Protein Science

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In order to survive extreme drying (anhydrobiosis), many organisms, spanning every kingdom of life, accumulate intrinsically disordered proteins (IDPs). For decades, the ability of anhydrobiosis‐related IDPs to form transient amphipathic helices has been suggested to be important for promoting desiccation tolerance. However, evidence empirically supporting the necessity and/or sufficiency of helicity in mediating anhydrobiosis is lacking. Here we demonstrate that the linker region of CAHS D, a desiccation‐related IDP from the tardigrade Hypsibius exemplaris, that contains significant helical structure, is the protective portion of this protein. Perturbing the sequence composition and grammar of the linker region of CAHS D, through the insertion of helix‐breaking prolines, modulating the identity of charged residues, or replacement of hydrophobic amino acids with serine or glycine residues results in variants with different degrees of helical structure. Importantly, correlation of protective capacity and helical content in variants generated through different helix perturbing modalities do not show as strong a trend, suggesting that while helicity is important it is not the only property that makes a protein protective during desiccation. These results provide direct evidence for the decades old theory that helicity of desiccation‐related IDPs is linked to their anhydrobiotic capacity.This article is protected by copyright. All rights reserved.

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Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity

Hernández‐Sánchez,

Rindfleisch,

Alpers

et al. 2024

Protein Science

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Intrinsically disordered late embryogenesis abundant (LEA) proteins play a central role in the tolerance of plants and other organisms to dehydration brought upon, for example, by freezing temperatures, high salt concentration, drought or desiccation, and many LEA proteins have been found to stabilize dehydration‐sensitive cellular structures. Their conformational ensembles are highly sensitive to the environment, allowing them to undergo conformational changes and adopt ordered secondary and quaternary structures and to participate in formation of membraneless organelles. In an interdisciplinary approach, we discovered how the functional diversity of the Arabidopsis thaliana LEA protein COR15A found in vitro is encoded in its structural repertoire, with the stabilization of membranes being achieved at the level of secondary structure and the stabilization of enzymes accomplished by the formation of oligomeric complexes. We provide molecular details on intra‐ and inter‐monomeric helix–helix interactions, demonstrate how oligomerization is driven by an α‐helical molecular recognition feature (α‐MoRF) and provide a rationale that the formation of noncanonical, loosely packed, right‐handed coiled‐coils might be a recurring theme for homo‐ and hetero‐oligomerization of LEA proteins.

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Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity – an X-ray and light scattering study

Abstract: The plant stress protein COR15A stabilizes chloroplast membranes during freezing.

Cited by 18 publications

References 60 publications

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

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

Helicity of a tardigrade disordered protein contributes to its protective function during desiccation

Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity

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