期刊
ARCHIVES OF MICROBIOLOGY
卷 191, 期 12, 页码 919-925出版社
SPRINGER
DOI: 10.1007/s00203-009-0516-5
关键词
Escherichia coli; Tat protein transport pathway; Signal peptidase I; LepB protein
类别
资金
- BBSRC [BB/C006844/2]
- Biotechnology and Biological Sciences Research Council [BB/C006844/2] Funding Source: researchfish
- Medical Research Council [G117/519] Funding Source: researchfish
- MRC [G117/519] Funding Source: UKRI
The twin-arginine translocation (Tat) apparatus is a protein targeting system found in the cytoplasmic membranes of many prokaryotes. Substrate proteins of the Tat pathway are synthesised with signal peptides bearing SRRxFLK 'twin-arginine' amino acid motifs. All Tat signal peptides have a common tripartite structure comprising a polar N-terminal region, followed by a hydrophobic region of variable length and a polar C-terminal region. In Escherichia coli, Tat signal peptides are proteolytically cleaved after translocation. The signal peptide C-terminal regions contain conserved AxA motifs, which are possible recognition sequences for leader peptidase I (LepB). In this work, the role of LepB in Tat signal peptide processing was addressed directly. Deliberate repression of lepB expression prevented processing of all Tat substrates tested, including SufI, AmiC, and a TorA-23K reporter protein. In addition, electron microscopy revealed gross defects in cell architecture and membrane integrity following depletion of cellular LepB protein levels.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据