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dc.contributor.authorLlorca, Oen_US
dc.contributor.authorMartin-Benito, Jen_US
dc.contributor.authorGrantham, Jen_US
dc.contributor.authorRitco-Vonsovici, Men_US
dc.contributor.authorWillison, KRen_US
dc.contributor.authorCarrascosa, JLen_US
dc.contributor.authorValpuesta, JMen_US
dc.date.accessioned2018-09-24T15:52:42Z
dc.date.issued2001-08-01en_US
dc.identifier15en_US
dc.identifier.citationEMBO JOURNAL, 2001, 20 pp. 4065 - 4075en_US
dc.identifier.issn0261-4189en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2840
dc.identifier.doi10.1093/emboj/20.15.4065en_US
dc.description.abstractFolding to completion of actin and tubulin in the eukaryotic cytosol requires their interaction with cytosolic chaperonin CCT [chaperonin containing tailless complex polypeptide 1 (TCP-1)]. Three-dimensional reconstructions of nucleotide-free CCT complexed to either actin or tubulin show that CCT stabilizes both cytoskeletal proteins in open and quasi-folded conformations mediated through interactions that are both subunit specific and geometry dependent. Here we find that upon ATP binding, mimicked by the non-hydrolysable analog AMP-PNP (5 ‘ -adenylylimido-diphosphate), to both CCT-alpha -actin and CCT-beta -tubulin complexes, the chaperonin component undergoes concerted movements of the apical domains, resulting in the cavity being closed off by the helical protrusions of the eight apical domains. However, in contrast to the GroE system, generation of this closed state does not induce the release of the substrate into the chaperonin cavity, and both cytoskeletal proteins remain bound to the chaperonin apical domains. Docking of the AMP-PNP-CCT-bound conformations of a-actin and P-tubulin to their respective native atomic structures suggests that both proteins have progressed towards their native states.en_US
dc.format.extent4065 - 4075en_US
dc.titleThe ‘sequential allosteric ring’ mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulinen_US
dc.typeJournal Article
rioxxterms.versionofrecord10.1093/emboj/20.15.4065en_US
rioxxterms.licenseref.startdate2001-08-01en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfEMBO JOURNALen_US
pubs.notesresearcherid-numbers: Valpuesta, Jose/T-1977-2017 Llorca, Oscar/K-1144-2014 Grantham, Julie/A-5002-2009 orcid-numbers: Valpuesta, Jose/0000-0001-7468-8053 Llorca, Oscar/0000-0001-5705-0699 unique-id: ISI:000170406600019en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Chromatin Regulation
pubs.volume20en_US
pubs.embargo.termsNot knownen_US
icr.researchteamChromatin Regulationen_US
dc.contributor.icrauthorWillison, Keithen_US


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