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dc.contributor.authorRivenzon-Segal, D
dc.contributor.authorWolf, SG
dc.contributor.authorShimon, L
dc.contributor.authorWillison, KR
dc.contributor.authorHorovitz, A
dc.date.accessioned2018-09-07T09:07:19Z
dc.date.issued2005-03
dc.identifier3
dc.identifier.citationNATURE STRUCTURAL & MOLECULAR BIOLOGY, 2005, 12 pp. 233 - 237
dc.identifier.issn1545-9985
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2591
dc.identifier.doi10.1038/nsmb901
dc.description.abstractThe eukaryotic cytoplasmic chaperonin containing TCP-1 (CCT) is a hetero-oligomeric complex that assists the folding of actins, tubulins and other proteins in an ATP- dependent manner. To understand the allosteric transitions that occur during the functional cycle of CCT, we imaged the chaperonin complex in the presence of different ATP concentrations. Labeling by monoclonal antibodies that bind specifically to the CCT and CCT subunits enabled alignment of all the CCT subunits of a given type in different particles. The analysis shows that the apo state of CCT has considerable apparent conformational heterogeneity that decreases with increasing ATP concentration. In contrast with the concerted allosteric switch of GroEL, ATP- induced conformational changes in CCT are found to spread around the ring in a sequential fashion that may facilitate domain- by-domain substrate folding. The approach described here can be used to unravel the allosteric mechanisms of other ring-shaped molecular machines.
dc.format.extent233 - 237
dc.languageeng
dc.language.isoeng
dc.titleSequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
dc.typeJournal Article
rioxxterms.versionofrecord10.1038/nsmb901
rioxxterms.licenseref.startdate2005-03
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfNATURE STRUCTURAL & MOLECULAR BIOLOGY
pubs.notesresearcherid-numbers: WOLF, SHARON/K-1768-2012 orcid-numbers: WOLF, SHARON/0000-0002-5337-5063 unique-id: ISI:000227345400014
pubs.notesNot known
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.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.volume12
pubs.embargo.termsNot known
icr.researchteamChromatin Regulationen_US
dc.contributor.icrauthorWillison, Keithen


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