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Remnant signal peptides on non-exported enzymes

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Remnant signal peptides on non-exported enzymes : implications for the evolution of prokaryotic respiratory chains. / Ize, Berengere; Coulthurst, Sarah J.; Hatzixanthis, Kostas; Caldelari, Isabelle; Buchanan, Grant; Barclay, Elaine C.; Richardson, David J.; Palmer, Tracy; Sargent, Frank.

In: Microbiology-SGM, Vol. 155, No. 12, 12.2009, p. 3992-4004.

Research output: Contribution to journalArticle

Harvard

Ize, B, Coulthurst, SJ, Hatzixanthis, K, Caldelari, I, Buchanan, G, Barclay, EC, Richardson, DJ, Palmer, T & Sargent, F 2009, 'Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains' Microbiology-SGM, vol 155, no. 12, pp. 3992-4004., 10.1099/mic.0.033647-0

APA

Ize, B., Coulthurst, S. J., Hatzixanthis, K., Caldelari, I., Buchanan, G., Barclay, E. C., ... Sargent, F. (2009). Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains. Microbiology-SGM, 155(12), 3992-4004. 10.1099/mic.0.033647-0

Vancouver

Ize B, Coulthurst SJ, Hatzixanthis K, Caldelari I, Buchanan G, Barclay EC et al. Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains. Microbiology-SGM. 2009 Dec;155(12):3992-4004. Available from: 10.1099/mic.0.033647-0

Author

Ize, Berengere; Coulthurst, Sarah J.; Hatzixanthis, Kostas; Caldelari, Isabelle; Buchanan, Grant; Barclay, Elaine C.; Richardson, David J.; Palmer, Tracy; Sargent, Frank / Remnant signal peptides on non-exported enzymes : implications for the evolution of prokaryotic respiratory chains.

In: Microbiology-SGM, Vol. 155, No. 12, 12.2009, p. 3992-4004.

Research output: Contribution to journalArticle

Bibtex - Download

@article{db5cbb9eddbd4f529fa866fc68b9aa3f,
title = "Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains",
keywords = "BIOTIN SULFOXIDE REDUCTASE, BACTERIAL 2-HYBRID SYSTEM, TWIN-ARGININE TRANSLOCASE, ESCHERICHIA-COLI, PROTEIN TRANSLOCATION, SALMONELLA-TYPHIMURIUM, NITRATE REDUCTASES, CHAPERONE, PATHWAY, GENE",
author = "Berengere Ize and Coulthurst, {Sarah J.} and Kostas Hatzixanthis and Isabelle Caldelari and Grant Buchanan and Barclay, {Elaine C.} and Richardson, {David J.} and Tracy Palmer and Frank Sargent",
year = "2009",
doi = "10.1099/mic.0.033647-0",
volume = "155",
number = "12",
pages = "3992--4004",
journal = "Microbiology-SGM",
issn = "1350-0872",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Remnant signal peptides on non-exported enzymes

T2 - implications for the evolution of prokaryotic respiratory chains

A1 - Ize,Berengere

A1 - Coulthurst,Sarah J.

A1 - Hatzixanthis,Kostas

A1 - Caldelari,Isabelle

A1 - Buchanan,Grant

A1 - Barclay,Elaine C.

A1 - Richardson,David J.

A1 - Palmer,Tracy

A1 - Sargent,Frank

AU - Ize,Berengere

AU - Coulthurst,Sarah J.

AU - Hatzixanthis,Kostas

AU - Caldelari,Isabelle

AU - Buchanan,Grant

AU - Barclay,Elaine C.

AU - Richardson,David J.

AU - Palmer,Tracy

AU - Sargent,Frank

PY - 2009/12

Y1 - 2009/12

N2 - <p>The twin-arginine translocation (Tat) pathway is a prokaryotic protein targeting system dedicated to the transmembrane translocation of folded proteins. Substrate proteins are directed to the Tat translocase by signal peptides bearing a conserved SRRxFLK 'twin-arginine' motif. In Escherichia coli, most of the 27 periplasmically located Tat substrates are cofactor-containing respiratory enzymes, and many of these harbour a molybdenum cofactor at their active site. Molybdenum cofactor-containing proteins are not exclusively located in the periplasm, however, with the major respiratory nitrate reductase (NarG) and the biotin sulfoxide reductase (BisC), for example, being located at the cytoplasmic side of the membrane. Interestingly, both NarG and Bisc contain 'N-tail' regions that bear some sequence similarity to twin-arginine signal peptides. In this work, we have examined the relationship between the non-exported N-tails and the Tat system. Using a sensitive genetic screen for Tat transport, variant N-tails were identified that displayed Tat transport activity. For the NarG 36-residue N-tail, six amino acid changes were needed to induce transport activity. However, these changes interfered with binding by the NarJ biosynthetic chaperone and impaired biosynthesis of the native enzyme. For the BisC 36-residue N-tail, only five amino acid substitutions were needed to restore Tat transport activity. These modifications also impaired in vivo BisC activity, but it was not possible to identify a biosynthetic chaperone for this enzyme. These data highlight an intimate genetic and evolutionary link between some non-exported redox enzymes and those transported across membranes by the Tat translocation system.</p>

AB - <p>The twin-arginine translocation (Tat) pathway is a prokaryotic protein targeting system dedicated to the transmembrane translocation of folded proteins. Substrate proteins are directed to the Tat translocase by signal peptides bearing a conserved SRRxFLK 'twin-arginine' motif. In Escherichia coli, most of the 27 periplasmically located Tat substrates are cofactor-containing respiratory enzymes, and many of these harbour a molybdenum cofactor at their active site. Molybdenum cofactor-containing proteins are not exclusively located in the periplasm, however, with the major respiratory nitrate reductase (NarG) and the biotin sulfoxide reductase (BisC), for example, being located at the cytoplasmic side of the membrane. Interestingly, both NarG and Bisc contain 'N-tail' regions that bear some sequence similarity to twin-arginine signal peptides. In this work, we have examined the relationship between the non-exported N-tails and the Tat system. Using a sensitive genetic screen for Tat transport, variant N-tails were identified that displayed Tat transport activity. For the NarG 36-residue N-tail, six amino acid changes were needed to induce transport activity. However, these changes interfered with binding by the NarJ biosynthetic chaperone and impaired biosynthesis of the native enzyme. For the BisC 36-residue N-tail, only five amino acid substitutions were needed to restore Tat transport activity. These modifications also impaired in vivo BisC activity, but it was not possible to identify a biosynthetic chaperone for this enzyme. These data highlight an intimate genetic and evolutionary link between some non-exported redox enzymes and those transported across membranes by the Tat translocation system.</p>

KW - BIOTIN SULFOXIDE REDUCTASE

KW - BACTERIAL 2-HYBRID SYSTEM

KW - TWIN-ARGININE TRANSLOCASE

KW - ESCHERICHIA-COLI

KW - PROTEIN TRANSLOCATION

KW - SALMONELLA-TYPHIMURIUM

KW - NITRATE REDUCTASES

KW - CHAPERONE

KW - PATHWAY

KW - GENE

U2 - 10.1099/mic.0.033647-0

DO - 10.1099/mic.0.033647-0

M1 - Article

JO - Microbiology-SGM

JF - Microbiology-SGM

SN - 1350-0872

IS - 12

VL - 155

SP - 3992

EP - 4004

ER -

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