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Open AccessArticle

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

1
Physical Biochemistry, University of Potsdam, Karl-Liebknecht-Str. 24–25, D-14476 Potsdam, Germany
2
Max-Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, D-14476 Potsdam, Germany
3
Department for Structural Biology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA
4
Max-Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, D-14476 Potsdam, Germany
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(8), 2794; https://doi.org/10.3390/ijms21082794
Received: 28 February 2020 / Revised: 15 April 2020 / Accepted: 16 April 2020 / Published: 17 April 2020
(This article belongs to the Special Issue Protein Intrinsic Disorder in Plant Biology)
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. View Full-Text
Keywords: IDP; LEA protein; abiotic stress; dehydration; conformational rearrangement; membrane stabilization; sequence-structure-function relationship IDP; LEA protein; abiotic stress; dehydration; conformational rearrangement; membrane stabilization; sequence-structure-function relationship
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MDPI and ACS Style

Knox-Brown, P.; Rindfleisch, T.; Günther, A.; Balow, K.; Bremer, A.; Walther, D.; Miettinen, M.S.; Hincha, D.K.; Thalhammer, A. Similar Yet Different–Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins. Int. J. Mol. Sci. 2020, 21, 2794. https://doi.org/10.3390/ijms21082794

AMA Style

Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. Similar Yet Different–Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins. International Journal of Molecular Sciences. 2020; 21(8):2794. https://doi.org/10.3390/ijms21082794

Chicago/Turabian Style

Knox-Brown, Patrick; Rindfleisch, Tobias; Günther, Anne; Balow, Kim; Bremer, Anne; Walther, Dirk; Miettinen, Markus S.; Hincha, Dirk K.; Thalhammer, Anja. 2020. "Similar Yet Different–Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins" Int. J. Mol. Sci. 21, no. 8: 2794. https://doi.org/10.3390/ijms21082794

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