Publication

Escherichia coli translocase: the unravelling of a molecular machine: the unravelling of a molecular machine

Manting, E. H. & Driessen, A. J. M., 2000, In : Molecular Microbiology. 37, 2, p. 226-238 13 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Manting, E. H., & Driessen, A. J. M. (2000). Escherichia coli translocase: the unravelling of a molecular machine: the unravelling of a molecular machine. Molecular Microbiology, 37(2), 226-238. https://doi.org/10.1046/j.1365-2958.2000.01980.x

Author

Manting, E.H ; Driessen, A.J.M. / Escherichia coli translocase: the unravelling of a molecular machine : the unravelling of a molecular machine. In: Molecular Microbiology. 2000 ; Vol. 37, No. 2. pp. 226-238.

Harvard

Manting, EH & Driessen, AJM 2000, 'Escherichia coli translocase: the unravelling of a molecular machine: the unravelling of a molecular machine', Molecular Microbiology, vol. 37, no. 2, pp. 226-238. https://doi.org/10.1046/j.1365-2958.2000.01980.x

Standard

Escherichia coli translocase: the unravelling of a molecular machine : the unravelling of a molecular machine. / Manting, E.H; Driessen, A.J.M.

In: Molecular Microbiology, Vol. 37, No. 2, 2000, p. 226-238.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Manting EH, Driessen AJM. Escherichia coli translocase: the unravelling of a molecular machine: the unravelling of a molecular machine. Molecular Microbiology. 2000;37(2):226-238. https://doi.org/10.1046/j.1365-2958.2000.01980.x


BibTeX

@article{cad8cf68391347f8aa5bd7286f610338,
title = "Escherichia coli translocase: the unravelling of a molecular machine: the unravelling of a molecular machine",
abstract = "Protein translocation across the bacterial cytoplasmic membrane has been studied extensively in Escherichia coli. The identification of the components involved and subsequent reconstitution of the purified translocation reaction have defined the minimal constituents that allowed extensive biochemical characterization of the so-called translocase. This functional enzyme complex consists of the SecYEG integral membrane protein complex and a peripherally bound ATPase, SecA. Under translocation conditions, four SecYEG heterotrimers assemble into one large protein complex, forming a putative protein-conducting channel. This tetrameric arrangement of SecYEG complexes and the highly dynamic SecA dimer together form a proton-motive force- and ATP-driven molecular machine that drives the stepwise translocation of targeted polypeptides across the cytoplasmic membrane. Recent findings concerning the translocase structure and mechanism of protein translocation are discussed and shine new light on controversies in the field.",
keywords = "SIGNAL-RECOGNITION PARTICLE, PRECURSOR PROTEIN TRANSLOCATION, PROTON MOTIVE FORCE, BACTERIAL CYTOPLASMIC MEMBRANE, ENDOPLASMIC-RETICULUM MEMBRANE, DISTINCT ATP-BINDING, DELTA-MU-H+, PREPROTEIN TRANSLOCASE, INNER-MEMBRANE, SECA PROTEIN",
author = "E.H Manting and A.J.M. Driessen",
note = "Relation: https://www.rug.nl/gbb/ date_submitted:2007 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute",
year = "2000",
doi = "10.1046/j.1365-2958.2000.01980.x",
language = "English",
volume = "37",
pages = "226--238",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley",
number = "2",

}

RIS

TY - JOUR

T1 - Escherichia coli translocase: the unravelling of a molecular machine

T2 - the unravelling of a molecular machine

AU - Manting, E.H

AU - Driessen, A.J.M.

N1 - Relation: https://www.rug.nl/gbb/ date_submitted:2007 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute

PY - 2000

Y1 - 2000

N2 - Protein translocation across the bacterial cytoplasmic membrane has been studied extensively in Escherichia coli. The identification of the components involved and subsequent reconstitution of the purified translocation reaction have defined the minimal constituents that allowed extensive biochemical characterization of the so-called translocase. This functional enzyme complex consists of the SecYEG integral membrane protein complex and a peripherally bound ATPase, SecA. Under translocation conditions, four SecYEG heterotrimers assemble into one large protein complex, forming a putative protein-conducting channel. This tetrameric arrangement of SecYEG complexes and the highly dynamic SecA dimer together form a proton-motive force- and ATP-driven molecular machine that drives the stepwise translocation of targeted polypeptides across the cytoplasmic membrane. Recent findings concerning the translocase structure and mechanism of protein translocation are discussed and shine new light on controversies in the field.

AB - Protein translocation across the bacterial cytoplasmic membrane has been studied extensively in Escherichia coli. The identification of the components involved and subsequent reconstitution of the purified translocation reaction have defined the minimal constituents that allowed extensive biochemical characterization of the so-called translocase. This functional enzyme complex consists of the SecYEG integral membrane protein complex and a peripherally bound ATPase, SecA. Under translocation conditions, four SecYEG heterotrimers assemble into one large protein complex, forming a putative protein-conducting channel. This tetrameric arrangement of SecYEG complexes and the highly dynamic SecA dimer together form a proton-motive force- and ATP-driven molecular machine that drives the stepwise translocation of targeted polypeptides across the cytoplasmic membrane. Recent findings concerning the translocase structure and mechanism of protein translocation are discussed and shine new light on controversies in the field.

KW - SIGNAL-RECOGNITION PARTICLE

KW - PRECURSOR PROTEIN TRANSLOCATION

KW - PROTON MOTIVE FORCE

KW - BACTERIAL CYTOPLASMIC MEMBRANE

KW - ENDOPLASMIC-RETICULUM MEMBRANE

KW - DISTINCT ATP-BINDING

KW - DELTA-MU-H+

KW - PREPROTEIN TRANSLOCASE

KW - INNER-MEMBRANE

KW - SECA PROTEIN

U2 - 10.1046/j.1365-2958.2000.01980.x

DO - 10.1046/j.1365-2958.2000.01980.x

M3 - Article

VL - 37

SP - 226

EP - 238

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 2

ER -

ID: 1215469