HEMOLYSIN SECRETION FROM ESCHERICHIA-COLI

被引：73

作者：

HOLLAND, IB

KENNY, B

BLIGHT, M

机构：

[1] Department of Genetics, University of Leicester, Adrian Builing, Reicester LE1 7RH, University Road

来源：

BIOCHIMIE | 1990年 / 72卷 / 2-3期

关键词：

haemolysi; P-glycoprotein; secretion; secretion signal;

D O I：

10.1016/0300-9084(90)90138-7

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：

Haemolysin (HlyA) secretion from E coli is directed by a specific C-terminal targeting signal, located within the last 27-50 amino acids, with quite novel characteristics. The HlyA molecule is secreted directly to the medium without a periplasmic intermediate or detectable proteolytic processing. The C-terminal domain of HlyA can also be used to promote the secretion of several other E coli and mammalian proteins. HlyD and HlyB are essential for translocation of HlyA to the medium and we propose that these proteins form a transenvelope complex which initially binds the HlyA signal followed by transport of HlyA to the medium. HlyB is a member of a family of membrane proteins engaged in ATP dependent secretion mechanisms conserved in many organisms including man (P-glycoprotein and the CF protein). In this review we discuss the structure, function and regulation of the secretion mechanism. © 1990.

引用

页码：131 / 141

页数：11

共 57 条

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BAKER K, 1987, THESIS U LEICESTER

[2]

Bayer M.E., 1979, BACTERIAL OUTER MEMB, P167

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