The secondary structure of the ferredoxin transit sequence is modulated by its interaction with negatively charged lipids

FEBS Letters

Pilon, Marinus¹  de Kruijff, Ben²  van't Hof, Ron²  Horniak, Ladislav³ 

[1]Department of Molecular Cell Biology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

[2]Department of Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

[3]Institute of Molecular and Subcellular Biology, Comenius University, Odborarske nam. 5, SK-811 07 Bratislava, Slovakia

关键词: Chloroplast protein import;    Transit peptide;    Circular dichroism;    Peptide conformation;    Lipid-protein interactions;    trfd;    transit peptide of ferredoxin;    C12-Pglycol;    dodecylphosphoglycol;    C14-Pglycol;    tetradecylphosphoglycol;    C12-PN;    dodecylphosphocholine;    C12-maltose;    dodecyl-β-D-maltose;    C10-glucose;    decyl-β-D-glucose;    lysoC16-PC;    1-palmitoyl-sn-glycero-3-phosphocholine;    lysoC14-PC;    1-myristoyl-sn-glycero-3-phosphocholine;    DHPC;    1;    2-diheptyl-sn-glycero-3-phosphocholine;    DOPC;    1;    2-dioleoyl-sn-glycero-3-phosphocholine;    DOPG;    1;    2-dioleoyl-sn-glycero-3-phosphoglycerol;    MGDG;    monogalactosyldiacylglycerol;    DGDG;    digalactosyldiacylglycerol;    SQDG;    sulphoquinovosyldiacylglycerol;    CD;    circular dichroism;    TLC;    thin layer chromatography;    SUVs;    small unilamellar vesicles;    CMC;    critical micelle concentration;   

DOI  :  10.1016/0014-5793(93)81720-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Import of proteins into chloroplasts depends on an N-terminal transit sequence. Transit sequences contain little primary sequence similarity and therefore recognition of these sequences is thought to involve specific folding. To assess the conformational flexibility of the transit sequence, we studied the transit peptide of preferredoxin (trfd) by circular dichroism. In buffer, trfd is in a random coil conformation. A large increase in α-helix was induced in the presence of micelles or vesicles formed by anionic lipids. Less pronounced changes in secondary structure were induced by zwitterionic detergents but no changes were observed in the presence of neutral detergents or vesicles composed of phosphatidylcholine.

【 授权许可】

Unknown