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Overlapping functions of components of a bacterial Sec-independent protein export pathway

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Overlapping functions of components of a bacterial Sec-independent protein export pathway. / Sargent, Frank; Bogsch, Erik G.; Stanley, Nicola R.; Wexler, Margaret; Robinson, Colin; Berks, Ben C.; Palmer, Tracy.

In: EMBO Journal, Vol. 17, No. 13, 1998, p. 3640-3650.

Research output: Contribution to journalArticle

Harvard

Sargent, F, Bogsch, EG, Stanley, NR, Wexler, M, Robinson, C, Berks, BC & Palmer, T 1998, 'Overlapping functions of components of a bacterial Sec-independent protein export pathway' EMBO Journal, vol 17, no. 13, pp. 3640-3650., 10.1093/emboj/17.13.3640

APA

Sargent, F., Bogsch, E. G., Stanley, N. R., Wexler, M., Robinson, C., Berks, B. C., & Palmer, T. (1998). Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO Journal, 17(13), 3640-3650. 10.1093/emboj/17.13.3640

Vancouver

Sargent F, Bogsch EG, Stanley NR, Wexler M, Robinson C, Berks BC et al. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO Journal. 1998;17(13):3640-3650. Available from: 10.1093/emboj/17.13.3640

Author

Sargent, Frank; Bogsch, Erik G.; Stanley, Nicola R.; Wexler, Margaret; Robinson, Colin; Berks, Ben C.; Palmer, Tracy / Overlapping functions of components of a bacterial Sec-independent protein export pathway.

In: EMBO Journal, Vol. 17, No. 13, 1998, p. 3640-3650.

Research output: Contribution to journalArticle

Bibtex - Download

@article{d48079e2457742b0a7b7d93fdecb7732,
title = "Overlapping functions of components of a bacterial Sec-independent protein export pathway",
author = "Frank Sargent and Bogsch, {Erik G.} and Stanley, {Nicola R.} and Margaret Wexler and Colin Robinson and Berks, {Ben C.} and Tracy Palmer",
year = "1998",
doi = "10.1093/emboj/17.13.3640",
volume = "17",
number = "13",
pages = "3640--3650",
journal = "EMBO Journal",
issn = "0261-4189",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Overlapping functions of components of a bacterial Sec-independent protein export pathway

A1 - Sargent,Frank

A1 - Bogsch,Erik G.

A1 - Stanley,Nicola R.

A1 - Wexler,Margaret

A1 - Robinson,Colin

A1 - Berks,Ben C.

A1 - Palmer,Tracy

AU - Sargent,Frank

AU - Bogsch,Erik G.

AU - Stanley,Nicola R.

AU - Wexler,Margaret

AU - Robinson,Colin

AU - Berks,Ben C.

AU - Palmer,Tracy

PY - 1998

Y1 - 1998

N2 - We describe the identification of two Escherichia coli genes required for the export of cofactor-containing periplasmic proteins, synthesized with signal peptides containing a twin arginine motif. Both gene products are homologous to the maize HCF106 protein required for the translocation of a subset of lumenal proteins across the thylakoid membrane. Disruption of either gene affects the export of a range of such proteins, and a complete block is observed when both genes are inactivated. The Sec protein export pathway was unaffected, indicating the involvement of the gene products in a novel export system. The accumulation of active cofactor-containing proteins in the cytoplasm of the mutant strains suggests a role for the gene products in the translocation of folded proteins. One of the two HCF106 homologues is encoded by the first gene of a four cistron operon, tatABCD, and the second by an unlinked gene, tatE. A mutation previously assigned to the hcf106 homologue encoded at the tatABCD locus, mttA, lies instead in the tatB gene.

AB - We describe the identification of two Escherichia coli genes required for the export of cofactor-containing periplasmic proteins, synthesized with signal peptides containing a twin arginine motif. Both gene products are homologous to the maize HCF106 protein required for the translocation of a subset of lumenal proteins across the thylakoid membrane. Disruption of either gene affects the export of a range of such proteins, and a complete block is observed when both genes are inactivated. The Sec protein export pathway was unaffected, indicating the involvement of the gene products in a novel export system. The accumulation of active cofactor-containing proteins in the cytoplasm of the mutant strains suggests a role for the gene products in the translocation of folded proteins. One of the two HCF106 homologues is encoded by the first gene of a four cistron operon, tatABCD, and the second by an unlinked gene, tatE. A mutation previously assigned to the hcf106 homologue encoded at the tatABCD locus, mttA, lies instead in the tatB gene.

U2 - 10.1093/emboj/17.13.3640

DO - 10.1093/emboj/17.13.3640

M1 - Article

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 13

VL - 17

SP - 3640

EP - 3650

ER -

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