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Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase

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Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase. / Maldonado , Barbara; Kneuper, Holger; Buchanan, Grant; Hatzixanthis, Kostas; Sargent, Frank; Berks, Ben C.; Palmer, Tracy.

In: FEBS Letters, Vol. 585, No. 3, 04.02.2011, p. 478-484.

Research output: Contribution to journalArticle

Harvard

Maldonado , B, Kneuper, H, Buchanan, G, Hatzixanthis, K, Sargent, F, Berks, BC & Palmer, T 2011, 'Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase' FEBS Letters, vol 585, no. 3, pp. 478-484.

APA

Maldonado , B., Kneuper, H., Buchanan, G., Hatzixanthis, K., Sargent, F., Berks, B. C., & Palmer, T. (2011). Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase. FEBS Letters, 585(3), 478-484doi: 10.1016/j.febslet.2011.01.016

Vancouver

Maldonado B, Kneuper H, Buchanan G, Hatzixanthis K, Sargent F, Berks BC et al. Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase. FEBS Letters. 2011 Feb 4;585(3):478-484.

Author

Maldonado , Barbara; Kneuper, Holger; Buchanan, Grant; Hatzixanthis, Kostas; Sargent, Frank; Berks, Ben C.; Palmer, Tracy / Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.

In: FEBS Letters, Vol. 585, No. 3, 04.02.2011, p. 478-484.

Research output: Contribution to journalArticle

Bibtex - Download

@article{35004315e0c74bedb566c39878b45780,
title = "Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase",
author = "Barbara Maldonado and Holger Kneuper and Grant Buchanan and Kostas Hatzixanthis and Frank Sargent and Berks, {Ben C.} and Tracy Palmer",
year = "2011",
volume = "585",
number = "3",
pages = "478--484",
journal = "FEBS Letters",
issn = "0014-5793",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase

A1 - Maldonado ,Barbara

A1 - Kneuper,Holger

A1 - Buchanan,Grant

A1 - Hatzixanthis,Kostas

A1 - Sargent,Frank

A1 - Berks,Ben C.

A1 - Palmer,Tracy

AU - Maldonado ,Barbara

AU - Kneuper,Holger

AU - Buchanan,Grant

AU - Hatzixanthis,Kostas

AU - Sargent,Frank

AU - Berks,Ben C.

AU - Palmer,Tracy

PY - 2011/2/4

Y1 - 2011/2/4

N2 - <p>The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function.</p><p>Structured summary:</p><p>TatA physically interacts with TatA by two hybrid (View interaction)</p><p>TatB and TatC bind by molecular sieving (View interaction)</p><p>TatB physically interacts with TatB by two hybrid (View Interaction 1, 2) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>

AB - <p>The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function.</p><p>Structured summary:</p><p>TatA physically interacts with TatA by two hybrid (View interaction)</p><p>TatB and TatC bind by molecular sieving (View interaction)</p><p>TatB physically interacts with TatB by two hybrid (View Interaction 1, 2) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>

KW - Protein transport

KW - Twin arginine signal peptide

KW - Tat pathway

KW - TatB

KW - Protein:protein interaction

KW - Mutagenesis

KW - SEC-INDEPENDENT PROTEIN

KW - CYSTEINE-SCANNING MUTAGENESIS

KW - BACTERIAL 2-HYBRID SYSTEM

KW - ESCHERICHIA-COLI

KW - TRANSPORT SYSTEM

KW - SIGNAL PEPTIDE

KW - EXPORT PATHWAY

KW - BINDING

KW - COMPLEXES

KW - RESIDUES

U2 - 10.1016/j.febslet.2011.01.016

DO - 10.1016/j.febslet.2011.01.016

M1 - Article

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

VL - 585

SP - 478

EP - 484

ER -

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