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OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity

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OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity. / Law, Christopher J; Penfold, Christopher N; Walker, Daniel C; Moore, Geoffrey R; James, Richard; Kleanthous, Colin.

In: FEBS Letters, Vol. 545, No. 2-3, 19.06.2003, p. 127-132.

Research output: Contribution to journalArticle

Harvard

Law, CJ, Penfold, CN, Walker, DC, Moore, GR, James, R & Kleanthous, C 2003, 'OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity', FEBS Letters, vol. 545, no. 2-3, pp. 127-132. https://doi.org/10.1016/S0014-5793(03)00511-8

APA

Law, C. J., Penfold, C. N., Walker, D. C., Moore, G. R., James, R., & Kleanthous, C. (2003). OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity. FEBS Letters, 545(2-3), 127-132. https://doi.org/10.1016/S0014-5793(03)00511-8

Vancouver

Law CJ, Penfold CN, Walker DC, Moore GR, James R, Kleanthous C. OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity. FEBS Letters. 2003 Jun 19;545(2-3):127-132. https://doi.org/10.1016/S0014-5793(03)00511-8

Author

Law, Christopher J ; Penfold, Christopher N ; Walker, Daniel C ; Moore, Geoffrey R ; James, Richard ; Kleanthous, Colin. / OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity. In: FEBS Letters. 2003 ; Vol. 545, No. 2-3. pp. 127-132.

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@article{4327355698054b368c52b1778d90873b,
title = "OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity",
abstract = "The outer membrane (OM) vitamin B-12 receptor, BtuB, is the primary receptor for E group colicin adsorption to Escherichia coli. Cell death by this family of toxins requires the OM porin OmpF but its role remains elusive. We show that OmpF enhances the ability of purified BtuB to protect bacteria against the endonuclease colicin E9, demonstrating either that the two OM proteins form the functional receptor or that OmpF is recruited for subsequent translocation of the bacteriocin. While stable binary colicin E9-BtuB complexes could be readily shown in vitro, OmpF-containing complexes could not be detected, implying that OmpF association with the BtuB-colicin complex, while necessary, must be weak and/or transient in nature. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.",
keywords = "BtuB, OmpF, porin, bacteriocin, colicin translocation, protein-protein interaction, OUTER-MEMBRANE, IMMUNITY PROTEIN, COBALAMIN TRANSPORTER, CRYSTAL-STRUCTURE, RECEPTOR PROTEIN, CROSS-RESISTANCE, UPTAKE SYSTEMS, LIPOPOLYSACCHARIDE, CRYSTALLIZATION, PURIFICATION",
author = "Law, {Christopher J} and Penfold, {Christopher N} and Walker, {Daniel C} and Moore, {Geoffrey R} and Richard James and Colin Kleanthous",
year = "2003",
month = "6",
day = "19",
doi = "10.1016/S0014-5793(03)00511-8",
language = "English",
volume = "545",
pages = "127--132",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2-3",

}

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TY - JOUR

T1 - OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity

AU - Law, Christopher J

AU - Penfold, Christopher N

AU - Walker, Daniel C

AU - Moore, Geoffrey R

AU - James, Richard

AU - Kleanthous, Colin

PY - 2003/6/19

Y1 - 2003/6/19

N2 - The outer membrane (OM) vitamin B-12 receptor, BtuB, is the primary receptor for E group colicin adsorption to Escherichia coli. Cell death by this family of toxins requires the OM porin OmpF but its role remains elusive. We show that OmpF enhances the ability of purified BtuB to protect bacteria against the endonuclease colicin E9, demonstrating either that the two OM proteins form the functional receptor or that OmpF is recruited for subsequent translocation of the bacteriocin. While stable binary colicin E9-BtuB complexes could be readily shown in vitro, OmpF-containing complexes could not be detected, implying that OmpF association with the BtuB-colicin complex, while necessary, must be weak and/or transient in nature. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

AB - The outer membrane (OM) vitamin B-12 receptor, BtuB, is the primary receptor for E group colicin adsorption to Escherichia coli. Cell death by this family of toxins requires the OM porin OmpF but its role remains elusive. We show that OmpF enhances the ability of purified BtuB to protect bacteria against the endonuclease colicin E9, demonstrating either that the two OM proteins form the functional receptor or that OmpF is recruited for subsequent translocation of the bacteriocin. While stable binary colicin E9-BtuB complexes could be readily shown in vitro, OmpF-containing complexes could not be detected, implying that OmpF association with the BtuB-colicin complex, while necessary, must be weak and/or transient in nature. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

KW - BtuB

KW - OmpF

KW - porin

KW - bacteriocin

KW - colicin translocation

KW - protein-protein interaction

KW - OUTER-MEMBRANE

KW - IMMUNITY PROTEIN

KW - COBALAMIN TRANSPORTER

KW - CRYSTAL-STRUCTURE

KW - RECEPTOR PROTEIN

KW - CROSS-RESISTANCE

KW - UPTAKE SYSTEMS

KW - LIPOPOLYSACCHARIDE

KW - CRYSTALLIZATION

KW - PURIFICATION

U2 - 10.1016/S0014-5793(03)00511-8

DO - 10.1016/S0014-5793(03)00511-8

M3 - Article

VL - 545

SP - 127

EP - 132

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2-3

ER -