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  Similar yet different–structural and functional diversity among Arabidopsis thaliana LEA_4 proteins

Knox-Brown, P., Rindfleisch, T., Günther, A., Balow, K., Bremer, A., Walther, D., et al. (2020). Similar yet different–structural and functional diversity among Arabidopsis thaliana LEA_4 proteins. International Journal of Molecular Sciences, 21(8): 2794. doi:10.3390/ijms21082794.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-4CF4-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-4CF5-1
Genre: Journal Article

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 Creators:
Knox-Brown, Patrick, Author
Rindfleisch, Tobias, Author
Günther, Anne, Author
Balow, Kim, Author
Bremer, Anne, Author
Walther, Dirk, Author
Miettinen, Markus S.1, Author              
Hincha, Dirk K., Author
Thalhammer, Anja, Author
Affiliations:
1Markus Miettinen, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_3070372              

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Free keywords: IDP; LEA protein; abiotic stress; dehydration; conformational rearrangement; membrane stabilization; sequence-structure-function relationship
 Abstract: 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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Language(s): eng - English
 Dates: 2020-04-172020
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.3390/ijms21082794
BibTex Citekey: ijms21082794
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Title: International Journal of Molecular Sciences
  Abbreviation : Int. J. Mol. Sci.
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI AG
Pages: - Volume / Issue: 21 (8) Sequence Number: 2794 Start / End Page: - Identifier: ISSN: 1422-0067