Discovery - University of Dundee - Online Publications

Library & Learning Centre

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site

Standard

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site. / Kneuper, H.; Maldonado, Barbara; Jager, Franziska; Buchanan, G.; Keller, R.; Palmer, T.; Krehenbrink, M.; Berks, B.C.; Müller, M.

In: Molecular Microbiology, Vol. 85, No. 5, 09.2012, p. 945-961.

Research output: Contribution to journalArticle

Harvard

Kneuper, H, Maldonado, B, Jager, F, Buchanan, G, Keller, R, Palmer, T, Krehenbrink, M, Berks, BC & Müller, M 2012, 'Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site' Molecular Microbiology, vol 85, no. 5, pp. 945-961.

APA

Kneuper, H., Maldonado, B., Jager, F., Buchanan, G., Keller, R., Palmer, T., Krehenbrink, M., Berks, B. C., & Müller, M. (2012). Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site. Molecular Microbiology, 85(5), 945-961doi: 10.1111/j.1365-2958.2012.08151.x

Vancouver

Kneuper H, Maldonado B, Jager F, Buchanan G, Keller R, Palmer T et al. Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site. Molecular Microbiology. 2012 Sep;85(5):945-961.

Author

Kneuper, H.; Maldonado, Barbara; Jager, Franziska; Buchanan, G.; Keller, R.; Palmer, T.; Krehenbrink, M.; Berks, B.C.; Müller, M. / Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.

In: Molecular Microbiology, Vol. 85, No. 5, 09.2012, p. 945-961.

Research output: Contribution to journalArticle

Bibtex - Download

@article{8891d4f7303044c5a802ed49b5e5023a,
title = "Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site",
author = "H. Kneuper and Barbara Maldonado and Franziska Jager and G. Buchanan and R. Keller and T. Palmer and M. Krehenbrink and B.C. Berks and M. Müller",
year = "2012",
volume = "85",
number = "5",
pages = "945--961",
journal = "Molecular Microbiology",
issn = "0950-382X",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site

A1 - Kneuper,H.

A1 - Maldonado,Barbara

A1 - Jager,Franziska

A1 - Buchanan,G.

A1 - Keller,R.

A1 - Palmer,T.

A1 - Krehenbrink,M.

A1 - Berks,B.C.

A1 - Müller,M.

AU - Kneuper,H.

AU - Maldonado,Barbara

AU - Jager,Franziska

AU - Buchanan,G.

AU - Keller,R.

AU - Palmer,T.

AU - Krehenbrink,M.

AU - Berks,B.C.

AU - Müller,M.

PY - 2012/9

Y1 - 2012/9

N2 - The twin arginine transport (Tat) system transports folded proteins across the prokaryotic cytoplasmic membrane and the plant thylakoid membrane. TatC is the largest and most conserved component of the Tat machinery. It forms a multisubunit complex with TatB and binds the signal peptides of Tat substrates. Here we have taken a random mutagenesis approach to identify substitutions in Escherichia coli TatC that inactivate protein transport. We identify 32 individual amino acid substitutions that abolish or severely compromise TatC activity. The majority of the inactivating substitutions fall within the first two periplasmic loops of TatC. These regions are predicted to have conserved secondary structure and results of extensive amino acid insertion and deletion mutagenesis are consistent with these conserved elements being essential for TatC function. Three inactivating substitutions were identified in the fifth transmembrane helix of TatC. The inactive M205R variant could be suppressed by mutations affecting amino acids in the transmembrane helix of TatB. A physical interaction between TatC helix 5 and the TatB transmembrane helix was confirmed by the formation of a site-specific disulphide bond between TatC M205C and TatB L9C variants. This is the first molecular contact site mapped to single amino acid level between these two proteins. © 2012 Blackwell Publishing Ltd.

AB - The twin arginine transport (Tat) system transports folded proteins across the prokaryotic cytoplasmic membrane and the plant thylakoid membrane. TatC is the largest and most conserved component of the Tat machinery. It forms a multisubunit complex with TatB and binds the signal peptides of Tat substrates. Here we have taken a random mutagenesis approach to identify substitutions in Escherichia coli TatC that inactivate protein transport. We identify 32 individual amino acid substitutions that abolish or severely compromise TatC activity. The majority of the inactivating substitutions fall within the first two periplasmic loops of TatC. These regions are predicted to have conserved secondary structure and results of extensive amino acid insertion and deletion mutagenesis are consistent with these conserved elements being essential for TatC function. Three inactivating substitutions were identified in the fifth transmembrane helix of TatC. The inactive M205R variant could be suppressed by mutations affecting amino acids in the transmembrane helix of TatB. A physical interaction between TatC helix 5 and the TatB transmembrane helix was confirmed by the formation of a site-specific disulphide bond between TatC M205C and TatB L9C variants. This is the first molecular contact site mapped to single amino acid level between these two proteins. © 2012 Blackwell Publishing Ltd.

UR - http://www.scopus.com/inward/record.url?partnerID=yv4JPVwI&eid=2-s2.0-84863745019&md5=6c20f7d63126bbb0316e4666d95d6ede

U2 - 10.1111/j.1365-2958.2012.08151.x

DO - 10.1111/j.1365-2958.2012.08151.x

M1 - Article

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 5

VL - 85

SP - 945

EP - 961

ER -

Documents

Library & Learning Centre

Contact | Accessibility | Policy