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Hsp90 Oligomers Interacting with the Aha1 Cochaperone: An Outlook for the Hsp90 Chaperone Machineries

Eléonore Lepvrier 1, 2 Laura Moullintraffort 3 Michaël Nigen 4 Renan Goude 5 Diane Allegro 6 Pascale Barbier 6 Vincent Peyrot 6 Daniel Thomas 3 Alexis Nazabal 7 Cyrille Garnier 3
1 Laboratoire de Pharmacie Galenique, Biopharmacie et Pharmacie Clinique
2 Irset - Institut de recherche en santé, environnement et travail
3 IGDR - Institut de Génétique et Développement de Rennes
4 UMR IATE - Ingénierie des Agro-polymères et Technologies Émergentes
5 Microbiologie : Risques Infectieux
6 CRO2 - Centre de Recherches en Oncologie biologique et Oncopharmacologie
7 Cova IX AG
Abstract : The 90-kDa heat shock protein (Hsp90) is a highly flexible dimer able to self-associate in the presence of divalent cations or under heat shock. This study investigated the relationship between Hsp90 oligomers and the Hsp90 cochaperone Aha1 (activator of Hsp90 ATPase). The interactions of Aha1 with Hsp90 dimers and oligomers were evaluated by ultracentrifugation, size-exclusion chromatography coupled to multiangle laser light scattering and high-mass matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Hsp90 dimer was able to bind up to four Aha1 molecules, and Hsp90 oligomers are also able to interact with Aha1. The binding of Aha1 did not interfere with the Hsp90 oligomerization process. Except for Hsp90 dimer, the stoichiometry of the interaction remained constant, at 2 Aha1 molecules per Hsp90 dimer, regardless of the degree of Hsp90 oligomerization. Moreover, Aha1 predominantly bound to Hsp90 oligomers. Thus, the ability of Hsp90 oligomers to bind the Aha1 ATPase activator reinforces their role within the Hsp90 chaperone machineries
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https://hal-univ-rennes1.archives-ouvertes.fr/hal-01175535
Contributor : Laurent Jonchère <>
Submitted on : Friday, July 10, 2015 - 3:54:12 PM
Last modification on : Friday, January 15, 2021 - 3:10:03 AM

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UNIV-RENNES1 | CNRS | IRSET | IGDR | UNIV-AMU | BIOSIT | NUMECAN | UR1-UFR-SVE | UNIV-ANGERS | UNIV-RENNES | INP-CSNP | PHARMA-AMU | INP | INRAE | IATE | CIRAD | UNIV-MONTPELLIER | MONTPELLIER-SUPAGRO | BA

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Eléonore Lepvrier, Laura Moullintraffort, Michaël Nigen, Renan Goude, Diane Allegro, et al.. Hsp90 Oligomers Interacting with the Aha1 Cochaperone: An Outlook for the Hsp90 Chaperone Machineries. Analytical Chemistry, American Chemical Society, 2015, 87 (14), pp.7043-7051. ⟨10.1021/acs.analchem.5b00051⟩. ⟨hal-01175535⟩

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