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

FEBS Letters

Dewar, Susan J¹  Dorazi, Robert¹ 

[1] Department of Biological Sciences, Heriot Watt University, Edinburgh EH14 4AS, UK

关键词: Topology;    Transmembrane;    Cell division;    FtsK;    PhoA;    Metalloprotease;   

DOI  :  10.1016/S0014-5793(00)01820-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 six 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.

【 授权许可】

Unknown