Biochimica et Biophysica Acta - Molecular Cell Research, volume 1843, issue 8, pages 1717-1731

Colicin import into E. coli cells: a model system for insights into the import mechanisms of bacteriocins.

Kim Young A. ¹

Tarr Alexander W. ¹

Penfold Christopher N. ¹

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School of Life Sciences, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, UK |

Publication type: Journal Article

Publication date: 2014-08-01

Elsevier

Journal: Biochimica et Biophysica Acta - Molecular Cell Research

Quartile SCImago

Quartile WOS

Impact factor: 5.1

ISSN: 01674889, 18792596

DOI: 10.1016/j.bbamcr.2014.04.010

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Molecular Biology

Cell Biology

Abstract

Bacteriocins are a diverse group of ribosomally synthesized protein antibiotics produced by most bacteria. They range from small lanthipeptides produced by lactic acid bacteria to much larger multi domain proteins of Gram negative bacteria such as the colicins from Escherichia coli . For activity bacteriocins must be released from the producing cell and then bind to the surface of a sensitive cell to instigate the import process leading to cell death. For over 50 years, colicins have provided a working platform for elucidating the structure/function studies of bacteriocin import and modes of action. An understanding of the processes that contribute to the delivery of a colicin molecule across two lipid membranes of the cell envelope has advanced our knowledge of protein–protein interactions (PPI), protein–lipid interactions and the role of order–disorder transitions of protein domains pertinent to protein transport. In this review, we provide an overview of the arrangement of genes that controls the synthesis and release of the mature protein. We examine the uptake processes of colicins from initial binding and sequestration of binding partners to crossing of the outer membrane, and then discuss the translocation of colicins through the cell periplasm and across the inner membrane to their cytotoxic site of action. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. • Colicin N binds LPS as its primary outer membrane receptor. • The intrinsically unstructured T domain (IUTD) passes through the lumen of OmpF. • The IUTD re-inserts through OmpF and tethers TolB via its interaction with TolB box. • Paradoxically, Immunity release from enzymatic colicins requires low forces. • Inner membrane processing of the nuclease domain of colicins is FtsH-dependent.

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Springer Nature	Springer Nature, 7, 15.91% Springer Nature 7 publications, 15.91%
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American Institute of Physics (AIP)	American Institute of Physics (AIP), 1, 2.27% American Institute of Physics (AIP) 1 publication, 2.27%
Portland Press	Portland Press, 1, 2.27% Portland Press 1 publication, 2.27%
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Biophysical Society	Biophysical Society, 1, 2.27% Biophysical Society 1 publication, 2.27%
American Chemical Society (ACS)	American Chemical Society (ACS), 1, 2.27% American Chemical Society (ACS) 1 publication, 2.27%
Dove Medical Press	Dove Medical Press, 1, 2.27% Dove Medical Press 1 publication, 2.27%
Novosibirsk State Agrarian University	Novosibirsk State Agrarian University, 1, 2.27% Novosibirsk State Agrarian University 1 publication, 2.27%
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Kim Y. A., Tarr A. W., Penfold C. Colicin import into E. coli cells: a model system for insights into the import mechanisms of bacteriocins. // Biochimica et Biophysica Acta - Molecular Cell Research. 2014. Vol. 1843. No. 8. pp. 1717-1731.

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RIS |

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RIS Copy

TY - JOUR

DO - 10.1016/j.bbamcr.2014.04.010

UR - https://doi.org/10.1016%2Fj.bbamcr.2014.04.010

TI - Colicin import into E. coli cells: a model system for insights into the import mechanisms of bacteriocins.

T2 - Biochimica et Biophysica Acta - Molecular Cell Research

AU - Kim, Young A.

AU - Tarr, Alexander W.

AU - Penfold, Christopher N.

PY - 2014

DA - 2014/08/01 00:00:00

PB - Elsevier

SP - 1717-1731

IS - 8

VL - 1843

SN - 0167-4889

SN - 1879-2596

ER -

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@article{2014_Kim,

author = {Young A. Kim and Alexander W. Tarr and Christopher N. Penfold},

title = {Colicin import into E. coli cells: a model system for insights into the import mechanisms of bacteriocins.},

journal = {Biochimica et Biophysica Acta - Molecular Cell Research},

year = {2014},

volume = {1843},

publisher = {Elsevier},

month = {aug},

url = {https://doi.org/10.1016%2Fj.bbamcr.2014.04.010},

number = {8},

pages = {1717--1731},

doi = {10.1016/j.bbamcr.2014.04.010}

}

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Kim, Young A., et al. “Colicin import into E. coli cells: a model system for insights into the import mechanisms of bacteriocins..” Biochimica et Biophysica Acta - Molecular Cell Research, vol. 1843, no. 8, Aug. 2014, pp. 1717-1731. https://doi.org/10.1016%2Fj.bbamcr.2014.04.010.

Found error?

Publisher

Elsevier

Journal

Biochimica et Biophysica Acta - Molecular Cell Research

Quartile SCImago

Quartile WOS

Impact factor

5.1

ISSN

01674889 (Print)
18792596 (Electronic)