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In vitro analysis of the bacterial twin-arginine-dependent protein export.

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In vitro analysis of the bacterial twin-arginine-dependent protein export. / Moser, Michael; Panahandeh, Sascha; Holzapfel, Eva; Müller, Matthias.

In: Methods Mol Biol, Vol. 390, 2007, p. 63-79.

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

Harvard

Moser, M, Panahandeh, S, Holzapfel, E & Müller, M 2007, 'In vitro analysis of the bacterial twin-arginine-dependent protein export.', Methods Mol Biol, vol. 390, pp. 63-79. <http://www.ncbi.nlm.nih.gov/pubmed/17951681?dopt=Citation>

APA

Moser, M., Panahandeh, S., Holzapfel, E., & Müller, M. (2007). In vitro analysis of the bacterial twin-arginine-dependent protein export. Methods Mol Biol, 390, 63-79. http://www.ncbi.nlm.nih.gov/pubmed/17951681?dopt=Citation

Vancouver

Moser M, Panahandeh S, Holzapfel E, Müller M. In vitro analysis of the bacterial twin-arginine-dependent protein export. Methods Mol Biol. 2007;390:63-79.

Bibtex

@article{2210998227ba41bc8ac3a595fed452b9,
title = "In vitro analysis of the bacterial twin-arginine-dependent protein export.",
abstract = "Prokaryotic organisms possess a specialized protein translocase in their cytoplasmic membranes that catalyzes the export of folded preproteins. Substrates for this pathway are distinguished by a twin-arginine consensus motif in their signal peptides (twin-arginine translocation [Tat] pathway). We have compiled detailed protocols for the preparation and operation of a cell-free system by which the bacterial Tat pathway can be fully reproduced in vitro. This system has proven useful and is being further exploited for the study of precursor-translocase interactions, assembly of the translocase, and the mechanism of transmembrane passage.",
author = "Michael Moser and Sascha Panahandeh and Eva Holzapfel and Matthias M{\"u}ller",
year = "2007",
language = "Deutsch",
volume = "390",
pages = "63--79",
journal = "Methods Mol Biol",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - In vitro analysis of the bacterial twin-arginine-dependent protein export.

AU - Moser, Michael

AU - Panahandeh, Sascha

AU - Holzapfel, Eva

AU - Müller, Matthias

PY - 2007

Y1 - 2007

N2 - Prokaryotic organisms possess a specialized protein translocase in their cytoplasmic membranes that catalyzes the export of folded preproteins. Substrates for this pathway are distinguished by a twin-arginine consensus motif in their signal peptides (twin-arginine translocation [Tat] pathway). We have compiled detailed protocols for the preparation and operation of a cell-free system by which the bacterial Tat pathway can be fully reproduced in vitro. This system has proven useful and is being further exploited for the study of precursor-translocase interactions, assembly of the translocase, and the mechanism of transmembrane passage.

AB - Prokaryotic organisms possess a specialized protein translocase in their cytoplasmic membranes that catalyzes the export of folded preproteins. Substrates for this pathway are distinguished by a twin-arginine consensus motif in their signal peptides (twin-arginine translocation [Tat] pathway). We have compiled detailed protocols for the preparation and operation of a cell-free system by which the bacterial Tat pathway can be fully reproduced in vitro. This system has proven useful and is being further exploited for the study of precursor-translocase interactions, assembly of the translocase, and the mechanism of transmembrane passage.

M3 - SCORING: Zeitschriftenaufsatz

VL - 390

SP - 63

EP - 79

JO - Methods Mol Biol

JF - Methods Mol Biol

SN - 1064-3745

ER -