Lipid—peptide interactions between fragments of the transit peptide of ribulose‐1,5‐bisphosphate carboxylase/oxygenase and chloroplast membrane lipids

FEBS Letters

Demel, Rudy A.¹  Keegstra, Kenneth²  de Kruijff, Ben¹  van't Hof, Ron¹ 

[1]Centre for Biomembranes and Lipid Enzymology, State University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands

[2]Department of Botany, University of Wisconsin, 436 Lincoln Drive, Madison, WI 53706 USA

关键词: Chloroplast protein import;    Transit peptide;    Peptide—lipid interaction;    Galactolipid;    Sulpholipid;    Small subunit of ribulose-1;    5-bisphosphate carboxylase/oxygenase;    prSS;    precursor of the small subunit of ribulose-1;    5-bisphosphate carboxylase/oxygenase;    MGDG;    monogalactosyl diacylglycerol;    DGDG;    digalactosyldiacylglycerol;    SQDG;    sulphoquinovosyl diacylglycerol;    DOPC;    diolcoyl-sn-glycero-3-phospholcholine;    DOPG;    1;    2-diolcoyl-sn-glycero-3-phosphoglycerol;    PIPES;    1;    4-piperazindiethane sulfonic acid;    HPLC;    high performance liquid chromatography;    HPTLC;    high performance thin layer chromatography;   

DOI  :  10.1016/0014-5793(91)81318-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interactions of fragments of the transit peptide of ribulose-1,5-bisphosphate carboxylase/oxygenase with lipid monolayers was studied in order to investigate the possible involvement of the membrane lipids in the protein import process. The fragments are surface active and have a differential ability to insert in lipid monolayers. The fragments have a preference for the chloroplast galacto- and sulpholipids and phosphatidylglycerol and interact with envelope membrane lipid extracts. These results suggest that probably transit peptide—lipid interactions are involved in the chloroplast protein import process.

【 授权许可】

Unknown