The lipid binding site of the phosphatidylcholine transfer protein from bovine liver
Author
van Loon, D.
Berkhout, Theo
Demel, R. A.
Wirtz, K. W. A.
Attention
2299/13690
Abstract
The phosphatidylcholine transfer protein (PC-TP) from bovine liver has a binding site for phosphatidylcholine (PC). Structural and molecular characteristics of this site were investigated by binding PC-analogues carrying photolabile, fluorescent and short-chain fatty acids. Analysis of the photolabeled PC/PC-TP adduct showed that the hydrophobic peptide segment Val171-Phe-Met-Tyr-Tyr-Phe-Asp177 is part of the lipid binding site for the 2-acyl chain. This site was further studied by binding PC carrying cis-parinaric acid at the sn-2-position. Time resolved fluorescence anisotropy measurements indicated that the 2-acyl chain was immobilized following the rotation of PC-TP. Similar experiments with PC carrying cis-parinaric acid at the sn-1-position demonstrated that the 1-acyl chain was immobilized as well but at a site distinctly different from that of the 2-acyl chain. Binding sites for the 1- and 2-acyl chain were then explored by use of PC-isomers carrying decanoic, lauric and myristic acid at the sn-1- (or sn-2-)-position and oleic acid at the sn-2- (or sn-1-)-position. Incubation with vesicles prepared of these PC-species indicated that binding to PC-TP diminished with decreasing acyl chain length but more so for species with short-chain fatty acids on the sn-2-position than on the sn-1-position. Transfer experiments confirmed that PC-TP discriminates between PC-isomers of apparently equal hydrophobicity favouring the transfer of these species carrying oleic acid at the sn-2-position.
Publication date
1985-08-30Published in
Chemistry and Physics of LipidsPublished version
https://doi.org/10.1016/0009-3084(85)90055-6Other links
http://hdl.handle.net/2299/13690Relations
School of Life and Medical SciencesMetadata
Show full item recordRelated items
Showing items related by title, author, creator and subject.
-
Sequence-specific, RNA-protein interactions overcome electrostatic barriers preventing assembly of satellite tobacco necrosis virus coat protein
Ford, Robert J.; Barker, Amy M.; Bakker, Saskia E.; Coutts, Robert H.A.; Ranson, Neil A.; Phillips, Simon E. V.; Pearson, Arwen R.; Stockley, Peter G. (2013-03-25)We have examined the roles of RNA-coat protein (CP) interactions in the assembly of satellite tobacco necrosis virus (STNV). The viral genomic RNA encodes only the CP, which comprises a β-barrel domain connected to a ... -
The tobacco necrosis virus p7a protein is a nucleic acid-binding protein
Offei, S.K.; Coffin, R.S.; Coutts, Robert H.A. (1995-06)The two centrally located open reading frames (ORFs) of necroviruses may, by analogy with the similarly located and related ORFs of carmoviruses, be expected to have a function in virus movement in plants. In the case of ... -
Potato yellow mosaic geminivirus AC2 protein is a sequence non-specific DNA binding protein
Sung, Y.K.; Coutts, Robert H.A. (1996-03-25)The AC2 protein of potato yellow mosaic geminivirus (PYMV) is by analogy with related geminiviruses thought to be a transcriptional activator protein. We have over-expressed the AC2 open reading frame in E. coli and purified ...