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<title lang=en>Hsp90 Oligomers Interacting with the Aha1 Cochaperone: An Outlook for the Hsp90 Chaperone Machineries</title>
<creator>Lepvrier, Eléonore</creator>
<creator>Moullintraffort, Laura</creator>
<creator>Nigen, Michaël</creator>
<creator>Goude, Renan</creator>
<creator>Allegro, Diane</creator>
<creator>Barbier, Pascale</creator>
<creator>Peyrot, Vincent</creator>
<creator>Thomas, Daniel</creator>
<creator>Nazabal, Alexis</creator>
<creator>Garnier, Cyrille</creator>
<contributor>Laboratoire de Pharmacie Galenique, Biopharmacie et Pharmacie Clinique ; Université de Rennes 1 (UR1)</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Institut de Génétique et Développement de Rennes (IGDR) ; Université de Rennes 1 (UR1) - Centre National de la Recherche Scientifique (CNRS) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Science et Technologie du Lait et de l'Oeuf (STLO) ; Institut National de la Recherche Agronomique (INRA) - AGROCAMPUS OUEST</contributor>
<contributor>Microbiologie : Risques Infectieux ; Université de Rennes 1 (UR1) - CHU Pontchaillou [Rennes] - Faculté de Chirurgie Dentaire de Rennes - Faculté d'Odontologie - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Centre de Recherches en Oncologie biologique et Oncopharmacologie (CRO2) ; Aix Marseille Université (AMU) - Hôpital de la Timone [CHU - APHM] (TIMONE) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Cova IX AG ; CovaIXAG</contributor>
<description>International audience</description>
<source>ISSN: 0003-2700</source>
<source>EISSN: 1520-6882</source>
<source>Analytical Chemistry</source>
<publisher>American Chemical Society</publisher>
<identifier>hal-01175535</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01175535</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01175535</source>
<source>Analytical Chemistry, American Chemical Society, 2015, 87 (14), pp.7043-7051. 〈10.1021/acs.analchem.5b00051〉</source>
<identifier>DOI : 10.1021/acs.analchem.5b00051</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.analchem.5b00051</relation>
<identifier>PUBMED : 26076190</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/26076190</relation>
<language>en</language>
<subject>[SDV] Life Sciences [q-bio]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>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</description>
<date>2015</date>
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