THE TRANSIT SEQUENCE OF A CHLOROPLAST PRECURSOR PROTEIN REORIENTS THE LIPIDS IN MONOGALACTOSYL DIGLYCERIDE CONTAINING BILAYERS

被引：16

作者：

CHUPIN, V ^{[1
]}

VANTHOF, R ^{[1
]}

DEKRUIJFF, B ^{[1
]}

机构：

[1] UNIV UTRECHT,CTR BIOMEMBRANES & LIPID ENZYMOL,DEPT MEMBRANE BIOCHEM,3584 CH UTRECHT,NETHERLANDS

来源：

FEBS LETTERS | 1994年 / 350卷 / 01期

关键词：

CHLOROPLAST; TRANSIT SEQUENCE; MONOGALACTOSYL DIGLYCERIDE; MEMBRANE STRUCTURE; H-2; NMR; P-31;

D O I：

10.1016/0014-5793(94)00734-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The interaction of the chloroplast precursor protein of ferredoxin with mixed model membranes composed of H-2 chain labeled monogalactosyl diacylglycerol and phosphatidylcholine was studied by H-2 and P-31 NMR. The bilayers were found to have special chain packing properties which most likely are the result of a specific arrangement of head groups at the interface. The precursor and not the corresponding apoprotein induced a bilayer-->isotropic transition in lipid organization as a result of the transit sequence-lipid interaction. The implications of these observations for proteins import into chloroplasts are indicated.

引用

页码：104 / 108

页数：5

共 28 条

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