DnaK functions as a central hub in the E. colichaperone network

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• dc.contributor.author Calloni, Giuliaca
• dc.contributor.author Chen, Taotaoca
• dc.contributor.author Schermann, Sonya M.ca
• dc.contributor.author Chang, Hung-chunca
• dc.contributor.author Genevaux, Pierreca
• dc.contributor.author Agostini, Federico, 1985-ca
• dc.contributor.author Tartaglia, Gian Gaetanoca
• dc.date.accessioned 2015-10-29T08:18:23Z
• dc.date.available 2015-10-29T08:18:23Z
• dc.date.issued 2012ca
• dc.description.abstract Cellular chaperone networks prevent potentially toxic protein aggregation and ensure proteome integrity. Here, we used Escherichia coli as a model to understand the organization of these networks, focusing on the cooperation of the DnaK system with the upstream chaperone Trigger factor (TF) and the downstream GroEL. Quantitative proteomics revealed that DnaK interacts with at least 700 mostly cytosolic proteins, including 180 relatively aggregation-prone proteins that utilize DnaK extensively during and after initial folding. Upon deletion of TF, DnaK interacts increasingly with ribosomal and other small, basic proteins, while its association with large multidomain proteins is reduced. DnaK also functions prominently in stabilizing proteins for subsequent folding by GroEL. These proteins accumulate on DnaK upon GroEL depletion and are then degraded, thus defining DnaK as a central organizer of the chaperone network. Combined loss of DnaK and TF causes proteostasis collapse with disruption of GroEL function, defective ribosomal biogenesis, and extensive aggregation of large proteins.
• dc.description.sponsorship The research leading to these results has received funding from EU Framework 7 Integrated Project PROSPECTS, the Deutsche Forschungsgemeinschaft (SFB 594), and the Körber Foundation is acknowledged. G.C. was supported by an EMBO long-term fellowship
• dc.format.mimetype application/pdfca
• dc.identifier.citation Calloni G, Chen T, Schermann SM, Chang HC, Genevaux P, Agostini F, et al. DnaK functions as a central hub in the E. coli chaperone network. Cell Rep. 2012 Mar 29;1(3):251-64. DOI: 10.1016/j.celrep.2011.12.007ca
• dc.identifier.doi http://dx.doi.org/10.1016/j.celrep.2011.12.007
• dc.identifier.issn 2211-1247ca
• dc.identifier.uri http://hdl.handle.net/10230/24950
• dc.language.iso engca
• dc.publisher Elsevierca
• dc.relation.ispartof Cell reports. 2012 Mar 29;1(3):251-64
• dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/201648
• dc.rights © 2012 The Authors. This is an Open Access article distributed under the terms of a Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc-nd/3.0/) which permits share, copy and redistribute the material in any medium or formatca
• dc.rights.accessRights info:eu-repo/semantics/openAccessca
• dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/
• dc.subject.other Escheríchia coli
• dc.subject.other Xaperonines
• dc.subject.other Proteïnes
• dc.title DnaK functions as a central hub in the E. colichaperone networkca
• dc.type info:eu-repo/semantics/articleca
• dc.type.version info:eu-repo/semantics/publishedVersionca