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The entire N-terminal half of TatC is involved in twin-arginine precursor binding.

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The entire N-terminal half of TatC is involved in twin-arginine precursor binding. / Holzapfel, Eva; Eisner, Gottfried; Alami, Meriem; Barrett, Claire M L; Buchanan, Grant; Lüke, Iris; Betton, Jean-Michel; Robinson, Colin; Palmer, Tracy; Moser, Michael; Müller, Matthias.

In: BIOCHEMISTRY-US, Vol. 46, No. 10, 10, 2007, p. 2892-2898.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Holzapfel, E, Eisner, G, Alami, M, Barrett, CML, Buchanan, G, Lüke, I, Betton, J-M, Robinson, C, Palmer, T, Moser, M & Müller, M 2007, 'The entire N-terminal half of TatC is involved in twin-arginine precursor binding.', BIOCHEMISTRY-US, vol. 46, no. 10, 10, pp. 2892-2898. <http://www.ncbi.nlm.nih.gov/pubmed/17300178?dopt=Citation>

APA

Holzapfel, E., Eisner, G., Alami, M., Barrett, C. M. L., Buchanan, G., Lüke, I., Betton, J-M., Robinson, C., Palmer, T., Moser, M., & Müller, M. (2007). The entire N-terminal half of TatC is involved in twin-arginine precursor binding. BIOCHEMISTRY-US, 46(10), 2892-2898. [10]. http://www.ncbi.nlm.nih.gov/pubmed/17300178?dopt=Citation

Vancouver

Holzapfel E, Eisner G, Alami M, Barrett CML, Buchanan G, Lüke I et al. The entire N-terminal half of TatC is involved in twin-arginine precursor binding. BIOCHEMISTRY-US. 2007;46(10):2892-2898. 10.

Bibtex

@article{7c4b027243e04eeab98a9f57b1ff3161,
title = "The entire N-terminal half of TatC is involved in twin-arginine precursor binding.",
abstract = "Translocation of twin-arginine precursor proteins across the cytoplasmic membrane of Escherichia coli requires the three membrane proteins TatA, TatB, and TatC. TatC and TatB were shown to be involved in precursor binding. We have analyzed in vitro a number of single alanine substitutions in tatC that were previously shown to compromise in vivo the function of the Tat translocase. All tatC mutants that were defective in precursor translocation into cytoplasmic membrane vesicles concomitantly interfered with precursor binding not only to TatC but also to TatB. Hence structural changes of TatC that affect precursor targeting simultaneously abolish engagement of the twin-arginine signal sequence with TatB and block the formation of a functional Tat translocase. Since these phenotypes were observed for tatC mutations spread over the first half of TatC, this entire part of the molecule must globally be involved in precursor binding.",
author = "Eva Holzapfel and Gottfried Eisner and Meriem Alami and Barrett, {Claire M L} and Grant Buchanan and Iris L{\"u}ke and Jean-Michel Betton and Colin Robinson and Tracy Palmer and Michael Moser and Matthias M{\"u}ller",
year = "2007",
language = "Deutsch",
volume = "46",
pages = "2892--2898",
journal = "BIOCHEMISTRY-US",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "10",

}

RIS

TY - JOUR

T1 - The entire N-terminal half of TatC is involved in twin-arginine precursor binding.

AU - Holzapfel, Eva

AU - Eisner, Gottfried

AU - Alami, Meriem

AU - Barrett, Claire M L

AU - Buchanan, Grant

AU - Lüke, Iris

AU - Betton, Jean-Michel

AU - Robinson, Colin

AU - Palmer, Tracy

AU - Moser, Michael

AU - Müller, Matthias

PY - 2007

Y1 - 2007

N2 - Translocation of twin-arginine precursor proteins across the cytoplasmic membrane of Escherichia coli requires the three membrane proteins TatA, TatB, and TatC. TatC and TatB were shown to be involved in precursor binding. We have analyzed in vitro a number of single alanine substitutions in tatC that were previously shown to compromise in vivo the function of the Tat translocase. All tatC mutants that were defective in precursor translocation into cytoplasmic membrane vesicles concomitantly interfered with precursor binding not only to TatC but also to TatB. Hence structural changes of TatC that affect precursor targeting simultaneously abolish engagement of the twin-arginine signal sequence with TatB and block the formation of a functional Tat translocase. Since these phenotypes were observed for tatC mutations spread over the first half of TatC, this entire part of the molecule must globally be involved in precursor binding.

AB - Translocation of twin-arginine precursor proteins across the cytoplasmic membrane of Escherichia coli requires the three membrane proteins TatA, TatB, and TatC. TatC and TatB were shown to be involved in precursor binding. We have analyzed in vitro a number of single alanine substitutions in tatC that were previously shown to compromise in vivo the function of the Tat translocase. All tatC mutants that were defective in precursor translocation into cytoplasmic membrane vesicles concomitantly interfered with precursor binding not only to TatC but also to TatB. Hence structural changes of TatC that affect precursor targeting simultaneously abolish engagement of the twin-arginine signal sequence with TatB and block the formation of a functional Tat translocase. Since these phenotypes were observed for tatC mutations spread over the first half of TatC, this entire part of the molecule must globally be involved in precursor binding.

M3 - SCORING: Zeitschriftenaufsatz

VL - 46

SP - 2892

EP - 2898

JO - BIOCHEMISTRY-US

JF - BIOCHEMISTRY-US

SN - 0006-2960

IS - 10

M1 - 10

ER -