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

Clémence Collet, Jenny-Lee Thomassin, Olivera Francetic, Pierre Genevaux and Guy Tran Van Nhieu ()
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Clémence Collet: Equipe Communication Intercellulaire et Infections Microbiennes. Centre de Recherche Interdisciplinaire en Biologie (CIRB). Collège de France
Jenny-Lee Thomassin: Equipe Communication Intercellulaire et Infections Microbiennes. Centre de Recherche Interdisciplinaire en Biologie (CIRB). Collège de France
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

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04414-2

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