SECA OF ESCHERICHIA-COLI TRAVERSES LIPID BILAYER OF PHOSPHOLIPID-VESICLES

被引:26
作者
AHN, T
KIM, H
机构
[1] Korea Adv Inst Sci and Technol, Dept Life Sci, Taejon, 305701
关键词
D O I
10.1006/bbrc.1994.2185
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
SecA protein of Escherichia coli, when added externally to the vesicles composed of phosphatidylethanolamine, dioleoylphosphatidylglycerol and cardiolipin, was found to be fragmented by trypsin encapsulated within the vesicles. In the presence of ATP or its non-hydrolyzing analogue, ATP-gamma S, the number of fragments and extent of hydrolysis occurred much less than in the absence of these compounds. When ADP was added, however, the hydrolysis products were similar to those when no nucleotide was present. Quenching of SecA fluorescence by vesicle-entrapped iodide corroborated the digestion results. These experiments demonstrated that the SecA protein traverses the lipid bilayer and its membrane topology depends on the kind of nucleotide present. (C) 1994 Academic Press, Inc.
引用
收藏
页码:326 / 330
页数:5
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