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Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria

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  • Patrice Rassam

    (University of Oxford
    University of York)

  • Nikki A. Copeland

    (University of York
    †Present addresses: Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK (N.A.C.); Biomedica Slovakia s.r.o., Drobného 27, 841 01 Bratislava, Slovakia (C.T.); School of Biochemistry, Medical Sciences Building, University Walk, Clifton, Bristol BS8 1TD, UK (S.J.C.); medi | Zentrum für medizinische Bildung, Max-Daetwyler-Platz 2, 3014 Bern, Switzerland (U.S.); Basil Hetzel Institute, Adelaide University, Woodville Road, Adelaide, South Australia 5011, Australia (T.J.G.))

  • Oliver Birkholz

    (University of Osnabrück)

  • Csaba Tóth

    (University of York
    †Present addresses: Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK (N.A.C.); Biomedica Slovakia s.r.o., Drobného 27, 841 01 Bratislava, Slovakia (C.T.); School of Biochemistry, Medical Sciences Building, University Walk, Clifton, Bristol BS8 1TD, UK (S.J.C.); medi | Zentrum für medizinische Bildung, Max-Daetwyler-Platz 2, 3014 Bern, Switzerland (U.S.); Basil Hetzel Institute, Adelaide University, Woodville Road, Adelaide, South Australia 5011, Australia (T.J.G.))

  • Matthieu Chavent

    (University of Oxford)

  • Anna L. Duncan

    (University of Oxford)

  • Stephen J. Cross

    (University of York
    †Present addresses: Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK (N.A.C.); Biomedica Slovakia s.r.o., Drobného 27, 841 01 Bratislava, Slovakia (C.T.); School of Biochemistry, Medical Sciences Building, University Walk, Clifton, Bristol BS8 1TD, UK (S.J.C.); medi | Zentrum für medizinische Bildung, Max-Daetwyler-Platz 2, 3014 Bern, Switzerland (U.S.); Basil Hetzel Institute, Adelaide University, Woodville Road, Adelaide, South Australia 5011, Australia (T.J.G.))

  • Nicholas G. Housden

    (University of Oxford)

  • Renata Kaminska

    (University of Oxford)

  • Urban Seger

    (University of York
    †Present addresses: Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK (N.A.C.); Biomedica Slovakia s.r.o., Drobného 27, 841 01 Bratislava, Slovakia (C.T.); School of Biochemistry, Medical Sciences Building, University Walk, Clifton, Bristol BS8 1TD, UK (S.J.C.); medi | Zentrum für medizinische Bildung, Max-Daetwyler-Platz 2, 3014 Bern, Switzerland (U.S.); Basil Hetzel Institute, Adelaide University, Woodville Road, Adelaide, South Australia 5011, Australia (T.J.G.))

  • Diana M. Quinn

    (University of York)

  • Tamsin J. Garrod

    (University of York
    †Present addresses: Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK (N.A.C.); Biomedica Slovakia s.r.o., Drobného 27, 841 01 Bratislava, Slovakia (C.T.); School of Biochemistry, Medical Sciences Building, University Walk, Clifton, Bristol BS8 1TD, UK (S.J.C.); medi | Zentrum für medizinische Bildung, Max-Daetwyler-Platz 2, 3014 Bern, Switzerland (U.S.); Basil Hetzel Institute, Adelaide University, Woodville Road, Adelaide, South Australia 5011, Australia (T.J.G.))

  • Mark S. P. Sansom

    (University of Oxford)

  • Jacob Piehler

    (University of Osnabrück)

  • Christoph G. Baumann

    (University of York)

  • Colin Kleanthous

    (University of Oxford)

Abstract

Fluorescent labelling is used to show that in E. coli, outer membrane protein (OMP) turnover is passive and binary in nature, and OMPs cluster to form islands in which diffusion of individual proteins is restricted owing to lateral interactions with other OMPs; new OMPs are inserted mostly at mid-cell, meaning that old OMP islands are displaced to the poles of growing cells.

Suggested Citation

  • Patrice Rassam & Nikki A. Copeland & Oliver Birkholz & Csaba Tóth & Matthieu Chavent & Anna L. Duncan & Stephen J. Cross & Nicholas G. Housden & Renata Kaminska & Urban Seger & Diana M. Quinn & Tamsin, 2015. "Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria," Nature, Nature, vol. 523(7560), pages 333-336, July.
    • Handle: RePEc:nat:nature:v:523:y:2015:i:7560:d:10.1038_nature14461
    DOI: 10.1038/nature14461
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    Cited by:

    1. Javier Abellon-Ruiz & Kalyanashis Jana & Augustinas Silale & Andrew M. Frey & Arnaud Baslé & Matthias Trost & Ulrich Kleinekathöfer & Bert Berg, 2023. "BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B12 uptake in gut Bacteroides," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Maik Müller & Fabienne Gräbnitz & Niculò Barandun & Yang Shen & Fabian Wendt & Sebastian N. Steiner & Yannik Severin & Stefan U. Vetterli & Milon Mondal & James R. Prudent & Raphael Hofmann & Marc Oos, 2021. "Light-mediated discovery of surfaceome nanoscale organization and intercellular receptor interaction networks," Nature Communications, Nature, vol. 12(1), pages 1-17, December.

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