RRC ID 11394
Author Hundertmark M, Dimova R, Lengefeld J, Seckler R, Hincha DK.
Title The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding.
Journal Biochim. Biophys. Acta
Abstract Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. Late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into β-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport.
Volume 1808(1)
Pages 446-53
Published 2011-1
DOI 10.1016/j.bbamem.2010.09.010
PII S0005-2736(10)00325-1
PMID 20875393
MeSH Arabidopsis / genetics* Arabidopsis Proteins / genetics Arabidopsis Proteins / metabolism Arabidopsis Proteins / physiology* Biophysics / methods Calorimetry / methods Electrophoresis, Polyacrylamide Gel Liposomes / chemistry Particle Size Plant Physiological Phenomena Protein Binding Protein Conformation Protein Folding Protein Structure, Secondary Recombinant Proteins / chemistry Time Factors
IF 3.498
Times Cited 24
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Arabidopsis / Cultured plant cells, genes pda07797