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

Navarro‐Retamal, Carlos; Bremer, Anne; Alzate‐Morales, Jans; Caballero, Julio; Hincha, Dirk K.; González, Wendy; Thalhammer, Anja

doi:10.1039/c6cp02272c

Cited by 28 publications

(67 citation statements)

References 79 publications

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“…). At the highest accessible concentration of 80% predominantly α‐helical structure was found in COR15A , 2H, and 4H (90%, 72%, and 89%, respectively), while α‐helicity in LEA25 and LEA11 only reached 63% and 50%, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…The proteins investigated here are not predicted to have such an arrangement of positively charged amino acids (see Fig. and ). In addition, FTIR spectroscopy showed no evidence for interactions of the proteins with the membrane lipid phosphate groups.…”

Section: Discussionmentioning

confidence: 94%

“…Error bars represent ± SEM from three different samples. Far‐ UV CD spectra and relative secondary structure content of COR 15A in the presence of increasing glycerol concentrations are not included in the figure because they were recently published .…”

Section: Resultsmentioning

confidence: 99%

“…In general, osmolytes stabilize folded proteins and induce folding of IDPs because they are preferentially excluded from the protein backbone, resulting in backbone dehydration . We have recently presented evidence from MD simulations that this is also the mechanism that stabilizes COR15A and B in an α‐helical conformation in the presence of glycerol by stabilizing intrabackbone H‐bonds at the expense of water‐backbone H‐bonds .…”

Section: Discussionmentioning

confidence: 99%

“…Such crowded conditions inside cells can be mimicked in vitro , e.g., by solutions containing increasing concentrations of glycerol . Such glycerol solutions induce folding in COR15A and stabilize the α‐helices of the protein .…”

Section: Introductionmentioning

confidence: 99%

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Folding of intrinsically disordered plant LEA proteins is driven by glycerol‐induced crowding and the presence of membranes

et al. 2017

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Late embryogenesis abundant (LEA) proteins are related to cellular dehydration tolerance. Most LEA proteins are predicted to have no stable secondary structure in solution, i.e., to be intrinsically disordered proteins (IDPs), but they may acquire α-helical structure upon drying. In the model plant Arabidopsis thaliana, the LEA proteins COR15A and COR15B are highly induced upon cold treatment and are necessary for the plants to attain full freezing tolerance. Freezing leads to increased intracellular crowding due to dehydration by extracellular ice crystals. In vitro, crowding by high glycerol concentrations induced partial folding of COR15 proteins. Here, we have extended these investigations to two related proteins, LEA11 and LEA25. LEA25 is much longer than LEA11 and COR15A, but shares a conserved central sequence domain with the other two proteins. We have created two truncated versions of LEA25 (2H and 4H) to elucidate the structural and functional significance of this domain. Light scattering and CD spectroscopy showed that all five proteins were largely unstructured and monomeric in dilute solution. They folded in the presence of increasing concentrations of trifluoroethanol and glycerol. Additional folding was observed in the presence of glycerol and membranes. Fourier transform infra red spectroscopy revealed an interaction of the LEA proteins with membranes in the dry state leading to a depression in the gel to liquid-crystalline phase transition temperature. Liposome stability assays revealed a cryoprotective function of the proteins. The C- and N-terminal extensions of LEA25 were important in cryoprotection, as the central domain itself (2H, 4H) only provided a low level of protection.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Folding of intrinsically disordered plant LEA proteins is driven by glycerol‐induced crowding and the presence of membranes

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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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A systematic review of chromogranin A (CgA) and its biomedical applications, unveiling its structure-related functions

Choi

Han

Kim

2021

J. Korean Phys. Soc.

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Chromogranin A (CgA), which is an intrinsically disordered protein that belongs to the granin family, was first discovered in the bovine adrenal medulla, and later identified in various organs. Under certain physiological conditions, CgA is cleaved into functionally diverse peptides, such as vasostatin-1, pancreastatin, and catestatin. In this review, we first describe the historical and systematic challenges for elucidating the molecular structures of CgA and its derived peptides and give a perspective of utilizing emerging techniques through integrative approaches. Subsequently, we review specific biological processes associated with CgA and its derived peptides in the neuroendocrine, immune, and digestive systems. Finally, we discuss biomedical applications of CgA as a biomarker, suggesting future directions toward translational and precision medicine.

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

Cited by 28 publications

References 79 publications

Folding of intrinsically disordered plant LEA proteins is driven by glycerol‐induced crowding and the presence of membranes

Folding of intrinsically disordered plant LEA proteins is driven by glycerol‐induced crowding and the presence of membranes

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

A systematic review of chromogranin A (CgA) and its biomedical applications, unveiling its structure-related functions

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