ANALYSIS OF THE MEMBRANE ORGANIZATION OF AN ESCHERICHIA-COLI PROTEIN TRANSLOCATOR, HLYB, A MEMBER OF A LARGE FAMILY OF PROKARYOTE AND EUKARYOTE SURFACE TRANSPORT PROTEINS

被引:107
作者
WANG, RC
SEROR, SJ
BLIGHT, M
PRATT, JM
BROOMESMITH, JK
HOLLAND, IB
机构
[1] UNIV PARIS 11, CNRS, URA 1354, INST GENET & MICROBIOL, F-91405 ORSAY, FRANCE
[2] UNIV LIVERPOOL, DEPT BIOCHEM, LIVERPOOL L69 3BX, ENGLAND
[3] UNIV SUSSEX, SCH BIOL SCI, BRIGHTON BN1 9RH, E SUSSEX, ENGLAND
[4] UNIV LEICESTER, DEPT GENET, LEICESTER LE1 7RH, ENGLAND
关键词
D O I
10.1016/0022-2836(91)90748-U
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 B (HlyB) is essential for secretion of the 107 × 103 Mr haemolysin A protein from Escherichia coli and is a member of a family of highly conserved, apparently ATP-dependent surface proteins in many organisms. We have shown in this study that both HlyB and HlyD fractionate primarily with the cytoplasmic membrane of E. coli and are accessible to proteases after removal of the outer membrane. We have measured experimentally the topological organization of HlyB within the membrane by construction of fusions to β-lactamase as a reporter. The predicted folding of HlyB, with a minimum of six transmembrane segments, does not always coincide with regions of highest average hydrophobicity. This suggests that HlyB may have a novel organization within the bilayer. From our data and comparative sequence analysis, we have been able to predict very similar topological models for the other members of the HlyB family. © 1991.
引用
收藏
页码:441 / 454
页数:14
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