Discovery - University of Dundee - Online Publications

Library & Learning Centre

Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies

Standard

Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies. / Widdick, David A.; Hicks, Matthew G.; Thompson, Benjamin J.; Tschumi, Andreas; Chandra, Govind; Sutcliffe, Iain C.; Bruelle, Juliane K.; Sander, Peter; Palmer, Tracy; Hutchings, Matthew I.

In: Molecular Microbiology, Vol. 80, No. 5, 06.2011, p. 1395-1412.

Research output: Contribution to journalArticle

Harvard

Widdick, DA, Hicks, MG, Thompson, BJ, Tschumi, A, Chandra, G, Sutcliffe, IC, Bruelle, JK, Sander, P, Palmer, T & Hutchings, MI 2011, 'Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies' Molecular Microbiology, vol 80, no. 5, pp. 1395-1412., 10.1111/j.1365-2958.2011.07656.x

APA

Widdick, D. A., Hicks, M. G., Thompson, B. J., Tschumi, A., Chandra, G., Sutcliffe, I. C., ... Hutchings, M. I. (2011). Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies. Molecular Microbiology, 80(5), 1395-1412. 10.1111/j.1365-2958.2011.07656.x

Vancouver

Widdick DA, Hicks MG, Thompson BJ, Tschumi A, Chandra G, Sutcliffe IC et al. Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies. Molecular Microbiology. 2011 Jun;80(5):1395-1412. Available from: 10.1111/j.1365-2958.2011.07656.x

Author

Widdick, David A.; Hicks, Matthew G.; Thompson, Benjamin J.; Tschumi, Andreas; Chandra, Govind; Sutcliffe, Iain C.; Bruelle, Juliane K.; Sander, Peter; Palmer, Tracy; Hutchings, Matthew I. / Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies.

In: Molecular Microbiology, Vol. 80, No. 5, 06.2011, p. 1395-1412.

Research output: Contribution to journalArticle

Bibtex - Download

@article{7d5f4bbd87014ec49fc846bbd03ce72e,
title = "Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies",
keywords = "OUTER-MEMBRANE, MYCOBACTERIUM-TUBERCULOSIS, ESCHERICHIA-COLI, PROTEINS, COELICOLOR, VIRULENCE, ACTINOBACTERIA, IDENTIFICATION, BIOSYNTHESIS, EXPRESSION",
author = "Widdick, {David A.} and Hicks, {Matthew G.} and Thompson, {Benjamin J.} and Andreas Tschumi and Govind Chandra and Sutcliffe, {Iain C.} and Bruelle, {Juliane K.} and Peter Sander and Tracy Palmer and Hutchings, {Matthew I.}",
year = "2011",
doi = "10.1111/j.1365-2958.2011.07656.x",
volume = "80",
number = "5",
pages = "1395--1412",
journal = "Molecular Microbiology",
issn = "0950-382x",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies

A1 - Widdick,David A.

A1 - Hicks,Matthew G.

A1 - Thompson,Benjamin J.

A1 - Tschumi,Andreas

A1 - Chandra,Govind

A1 - Sutcliffe,Iain C.

A1 - Bruelle,Juliane K.

A1 - Sander,Peter

A1 - Palmer,Tracy

A1 - Hutchings,Matthew I.

AU - Widdick,David A.

AU - Hicks,Matthew G.

AU - Thompson,Benjamin J.

AU - Tschumi,Andreas

AU - Chandra,Govind

AU - Sutcliffe,Iain C.

AU - Bruelle,Juliane K.

AU - Sander,Peter

AU - Palmer,Tracy

AU - Hutchings,Matthew I.

PY - 2011/6

Y1 - 2011/6

N2 - <p>P&gt;Following translocation, bacterial lipoproteins are lipidated by lipoprotein diacylglycerol transferase (Lgt) and cleaved of their signal peptides by lipoprotein signal peptidase (Lsp). In Gram-negative bacteria and mycobacteria, lipoproteins are further lipidated by lipoprotein N-acyl transferase (Lnt), to give triacylated lipoproteins. Streptomyces are unusual amongst Gram-positive bacteria because they export large numbers of lipoproteins via the twin arginine protein transport (Tat) pathway. Furthermore, some Streptomyces species encode two Lgt homologues and all Streptomyces species encode two homologues of Lnt. Here we characterize lipoprotein biogenesis in the plant pathogen Streptomyces scabies and report that lgt and lsp mutants are defective in growth and development while only moderately affected in virulence. Lipoproteins are lost from the membrane in an S. scabies lgt mutant but restored by expression of Streptomyces coelicolor lgt1 or lgt2 confirming that both encode functional Lgt enzymes. Furthermore, lipoproteins are N-acylated in Streptomyces with efficient N-acylation dependent on Lnt1 and Lnt2. However, deletion of lnt1 and lnt2 has no effect on growth, development or virulence. We thus present a detailed study of lipoprotein biogenesis in Streptomyces, the first study of Lnt function in a monoderm bacterium and the first study of bacterial lipoproteins as virulence factors in a plant pathogen.</p>

AB - <p>P&gt;Following translocation, bacterial lipoproteins are lipidated by lipoprotein diacylglycerol transferase (Lgt) and cleaved of their signal peptides by lipoprotein signal peptidase (Lsp). In Gram-negative bacteria and mycobacteria, lipoproteins are further lipidated by lipoprotein N-acyl transferase (Lnt), to give triacylated lipoproteins. Streptomyces are unusual amongst Gram-positive bacteria because they export large numbers of lipoproteins via the twin arginine protein transport (Tat) pathway. Furthermore, some Streptomyces species encode two Lgt homologues and all Streptomyces species encode two homologues of Lnt. Here we characterize lipoprotein biogenesis in the plant pathogen Streptomyces scabies and report that lgt and lsp mutants are defective in growth and development while only moderately affected in virulence. Lipoproteins are lost from the membrane in an S. scabies lgt mutant but restored by expression of Streptomyces coelicolor lgt1 or lgt2 confirming that both encode functional Lgt enzymes. Furthermore, lipoproteins are N-acylated in Streptomyces with efficient N-acylation dependent on Lnt1 and Lnt2. However, deletion of lnt1 and lnt2 has no effect on growth, development or virulence. We thus present a detailed study of lipoprotein biogenesis in Streptomyces, the first study of Lnt function in a monoderm bacterium and the first study of bacterial lipoproteins as virulence factors in a plant pathogen.</p>

KW - OUTER-MEMBRANE

KW - MYCOBACTERIUM-TUBERCULOSIS

KW - ESCHERICHIA-COLI

KW - PROTEINS

KW - COELICOLOR

KW - VIRULENCE

KW - ACTINOBACTERIA

KW - IDENTIFICATION

KW - BIOSYNTHESIS

KW - EXPRESSION

U2 - 10.1111/j.1365-2958.2011.07656.x

DO - 10.1111/j.1365-2958.2011.07656.x

M1 - Article

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382x

IS - 5

VL - 80

SP - 1395

EP - 1412

ER -

Documents

Library & Learning Centre

Contact | Accessibility | Policy