Membrane topology of the N-terminus of the Escherichia coli FtsK division protein

被引：26

作者：

Dorazi, R ^{[1
]}

Dewar, SJ ^{[1
]}

机构：

[1] Heriot Watt Univ, Dept Biol Sci, Edinburgh EH14 4AS, Midlothian, Scotland

来源：

FEBS LETTERS | 2000年 / 478卷 / 1-2期

基金：

英国生物技术与生命科学研究理事会;

关键词：

topology; transmembrane; cell division; FtsK; PhoA; metalloprotease;

D O I：

10.1016/S0014-5793(00)01820-2

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 Escherichia coli FtsK protein targets the septum, is essential for cell division and may play a role in DNA partitioning, Computer modelling suggests that the first 180 amino acids of the protein are embedded in the cytoplasmic membrane by up to sis transmembrane domains, We demonstrate, using gene fusions, that the N-terminus contains four transmembrane helices that link two periplasmic domains. The first periplasmic domain contains an HEXXH amino acid sequence characteristic of zinc metalloproteases, We show by mutation analysis that the conserved glutamic acid of the HEXXH sequence is essential for FtsK function during septation. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：13 / 18

页数：6

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