RRC ID 75830
Author Popova AV, Hundertmark M, Seckler R, Hincha DK.
Title Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes.
Journal Biochim Biophys Acta
Abstract Dehydration stress-related late embryogenesis abundant (LEA) proteins have been found in plants, invertebrates and bacteria. Most LEA proteins are unstructured in solution, but some fold into amphipathic α-helices during drying. The Pfam LEA_4 (Group 3) protein LEA7 from the higher plant Arabidopsis thaliana was predicted to be 87% α-helical, while CD spectroscopy showed it to be largely unstructured in solution and only 35% α-helical in the dry state. However, the dry protein contained 15% β-sheets. FTIR spectroscopy revealed the β-sheets to be largely due to aggregation. β-Sheet content was reduced and α-helix content increased when LEA7 was dried in the presence of liposomes with secondary structure apparently influenced by lipid composition. Secondary structure was also affected by the presence of membranes in the fully hydrated state. A temperature-induced increase in the flexibility of the dry protein was also only observed in the presence of membranes. Functional interactions of LEA7 with membranes in the dry state were indicated by its influence on the thermotropic phase transitions of the lipids and interactions with the lipid headgroup phosphates.
Volume 1808(7)
Pages 1879-87
Published 2011-7-1
DOI 10.1016/j.bbamem.2011.03.009
PII S0005-2736(11)00086-1
PMID 21443857
MeSH Amino Acid Sequence Arabidopsis Proteins / chemistry* Arabidopsis Proteins / genetics Cell Membrane / chemistry Circular Dichroism Desiccation* Molecular Sequence Data Protein Structure, Secondary Recombinant Proteins / chemistry Recombinant Proteins / genetics Sequence Homology, Amino Acid Spectroscopy, Fourier Transform Infrared
IF 3.411
Arabidopsis / Cultured plant cells, genes pda00834