| RRC ID |
75830
|
| 著者 |
Popova AV, Hundertmark M, Seckler R, Hincha DK.
|
| タイトル |
Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes.
|
| ジャーナル |
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.
|
| 巻・号 |
1808(7)
|
| ページ |
1879-87
|
| 公開日 |
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
|
| リソース情報 |
| シロイヌナズナ / 植物培養細胞・遺伝子 |
pda00834 |
