SECA OF ESCHERICHIA-COLI TRAVERSES LIPID BILAYER OF PHOSPHOLIPID-VESICLES
SECA OF ESCHERICHIA-COLI TRAVERSES LIPID BILAYER OF PHOSPHOLIPID-VESICLES
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DOI：
10.1006/bbrc.1994.2185
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发表时间：
1994-08-30
影响因子：
3.1
通讯作者：
KIM, H
中科院分区：
文献类型：
--
作者：
AHN, T;KIM, H
将大肠杆菌的SecA蛋白加入到由磷脂酰乙醇胺、二油基磷脂酰甘油和心磷脂组成的囊泡中，发现其被囊泡内的胰蛋白酶粉碎。在ATP或其非水解类似物ATP- γ S存在的情况下，发生水解的片段数量和程度要比没有这些化合物时少得多。然而，当ADP加入时，水解产物与不存在核苷酸时相似。囊泡包裹的碘化物猝灭SecA荧光证实了消解结果。这些实验表明，SecA蛋白穿过脂质双分子层，其膜拓扑结构取决于存在的核苷酸种类。(C) 1994学术出版社，Inc.
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.