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Protein polarization driven by nucleoid exclusion of DnaK(HSP70)–substrate complexes

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  • Clémence Collet

    (Equipe Communication Intercellulaire et Infections Microbiennes. Centre de Recherche Interdisciplinaire en Biologie (CIRB). Collège de France
    Institut National de la Santé et de la Recherche Médicale (Inserm) U1050
    Centre National de la Recherche Scientifique (CNRS) UMR7241
    MEMOLIFE Laboratory of excellence and Paris Science Lettre)

  • Jenny-Lee Thomassin

    (Equipe Communication Intercellulaire et Infections Microbiennes. Centre de Recherche Interdisciplinaire en Biologie (CIRB). Collège de France
    Institut National de la Santé et de la Recherche Médicale (Inserm) U1050
    Centre National de la Recherche Scientifique (CNRS) UMR7241
    MEMOLIFE Laboratory of excellence and Paris Science Lettre)

  • Olivera Francetic

    (Department of Structural Biology and Chemistry, CNRS UMR3528)

  • Pierre Genevaux

    (Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS)

  • Guy Tran Van Nhieu

    (Equipe Communication Intercellulaire et Infections Microbiennes. Centre de Recherche Interdisciplinaire en Biologie (CIRB). Collège de France
    Institut National de la Santé et de la Recherche Médicale (Inserm) U1050
    Centre National de la Recherche Scientifique (CNRS) UMR7241
    MEMOLIFE Laboratory of excellence and Paris Science Lettre)

Abstract

Many bacterial proteins require specific subcellular localization for function. How Escherichia coli proteins localize at one pole, however, is still not understood. Here, we show that the DnaK (HSP70) chaperone controls unipolar localization of the Shigella IpaC type III secretion substrate. While preventing the formation of lethal IpaC aggregates, DnaK promoted the incorporation of IpaC into large and dynamic complexes (LDCs) restricted at the bacterial pole through nucleoid occlusion. Unlike stable polymers and aggregates, LDCs show dynamic behavior indicating that nucleoid occlusion also applies to complexes formed through transient interactions. Fluorescence recovery after photobleaching analysis shows DnaK-IpaC exchanges between opposite poles and DnaKJE-mediated incorporation of immature substrates in LDCs. These findings reveal a key role for LDCs as reservoirs of functional DnaK-substrates that can be rapidly mobilized for secretion triggered upon bacterial contact with host cells.

Suggested Citation

  • Clémence Collet & Jenny-Lee Thomassin & Olivera Francetic & Pierre Genevaux & Guy Tran Van Nhieu, 2018. "Protein polarization driven by nucleoid exclusion of DnaK(HSP70)–substrate complexes," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04414-2
    DOI: 10.1038/s41467-018-04414-2
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