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

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Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. / Luke, Iris; Handford, Jennifer I.; Palmer, Tracy; Sargent, Frank.

In: Archives of Microbiology, Vol. 191, No. 12, 12.2009, p. 919-925.

Research output: Contribution to journalArticle

Harvard

Luke, I, Handford, JI, Palmer, T & Sargent, F 2009, 'Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB' Archives of Microbiology, vol 191, no. 12, pp. 919-925., 10.1007/s00203-009-0516-5

APA

Luke, I., Handford, J. I., Palmer, T., & Sargent, F. (2009). Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. Archives of Microbiology, 191(12), 919-925. 10.1007/s00203-009-0516-5

Vancouver

Luke I, Handford JI, Palmer T, Sargent F. Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. Archives of Microbiology. 2009 Dec;191(12):919-925. Available from: 10.1007/s00203-009-0516-5

Author

Luke, Iris; Handford, Jennifer I.; Palmer, Tracy; Sargent, Frank / Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB.

In: Archives of Microbiology, Vol. 191, No. 12, 12.2009, p. 919-925.

Research output: Contribution to journalArticle

Bibtex - Download

@article{a0fd8c23534d493c85042596c2e36f30,
title = "Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB",
keywords = "Escherichia coli, Tat protein transport pathway, Signal peptidase I, LepB protein, OUTER-MEMBRANE, EXPORT PATHWAY, PROTEIN TRANSLOCATION, CELL-ENVELOPE, EXPRESSION, INTEGRITY, PROMOTER, VECTORS, SYSTEM, OPERON",
author = "Iris Luke and Handford, {Jennifer I.} and Tracy Palmer and Frank Sargent",
year = "2009",
doi = "10.1007/s00203-009-0516-5",
volume = "191",
number = "12",
pages = "919--925",
journal = "Archives of Microbiology",
issn = "0302-8933",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB

A1 - Luke,Iris

A1 - Handford,Jennifer I.

A1 - Palmer,Tracy

A1 - Sargent,Frank

AU - Luke,Iris

AU - Handford,Jennifer I.

AU - Palmer,Tracy

AU - Sargent,Frank

PY - 2009/12

Y1 - 2009/12

N2 - <p>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.</p>

AB - <p>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.</p>

KW - Escherichia coli

KW - Tat protein transport pathway

KW - Signal peptidase I

KW - LepB protein

KW - OUTER-MEMBRANE

KW - EXPORT PATHWAY

KW - PROTEIN TRANSLOCATION

KW - CELL-ENVELOPE

KW - EXPRESSION

KW - INTEGRITY

KW - PROMOTER

KW - VECTORS

KW - SYSTEM

KW - OPERON

U2 - 10.1007/s00203-009-0516-5

DO - 10.1007/s00203-009-0516-5

M1 - Article

JO - Archives of Microbiology

JF - Archives of Microbiology

SN - 0302-8933

IS - 12

VL - 191

SP - 919

EP - 925

ER -

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