RRC ID 65783
Author Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A.
Title Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.
Journal Int J Mol Sci
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.
Volume 21(8)
Published 2020-4-17
DOI 10.3390/ijms21082794
PII ijms21082794
PMID 32316452
PMC PMC7215670
MeSH Arabidopsis / metabolism* Arabidopsis Proteins / chemistry* Arabidopsis Proteins / metabolism* Computational Biology / methods Models, Molecular Molecular Conformation Molecular Dynamics Simulation Protein Folding Stress, Physiological
IF 4.556
Arabidopsis / Cultured plant cells, genes pda00834