Archives of Microbiology

, Volume 191, Issue 12, pp 919–925

Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB

Authors

  • Iris Lüke
    • Division of Molecular Microbiology, College of Life SciencesUniversity of Dundee
  • Jennifer I. Handford
    • Department of Molecular MicrobiologyJohn Innes Centre
  • Tracy Palmer
    • Division of Molecular Microbiology, College of Life SciencesUniversity of Dundee
    • Division of Molecular Microbiology, College of Life SciencesUniversity of Dundee
Short Communication

DOI: 10.1007/s00203-009-0516-5

Cite this article as:
Lüke, I., Handford, J.I., Palmer, T. et al. Arch Microbiol (2009) 191: 919. doi:10.1007/s00203-009-0516-5

Abstract

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.

Keywords

Escherichia coliTat protein transport pathwaySignal peptidase ILepB protein

Copyright information

© Springer-Verlag 2009