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dc.contributor.authorShimon, Len_US
dc.contributor.authorHynes, GMen_US
dc.contributor.authorMcCormack, EAen_US
dc.contributor.authorWillison, KRen_US
dc.contributor.authorHorovitz, Aen_US
dc.date.accessioned2018-08-30T13:48:06Z
dc.date.issued2008-03-21en_US
dc.identifier2en_US
dc.identifier.citationJOURNAL OF MOLECULAR BIOLOGY, 2008, 377 pp. 469 - 477en_US
dc.identifier.issn0022-2836en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2453
dc.identifier.eissn1089-8638en_US
dc.identifier.doi10.1016/j.jmb.2008.01.011en_US
dc.description.abstractSaccharomyces cerevisiae yeast cells containing the chaperonin CCT (chaperonin-containing t-complex polypeptide 1 (TCP-1)) with the G345D mutation in subunit CCT4 (anc2-1) are temperature-sensitive for growth and display defects in organization of actin structure, budding and cell shape. In this first structure-function analysis of CCT, we show that this mutation abolishes both intra- and inter-ring cooperativity in ATP binding by CCT. The finding that a single mutation in only one subunit in each CCT ring has such drastic effects highlights the importance of allostery for its in vivo function. These results, together with other kinetic data for wild-type CCT reported in this study, provide support for the sequential model for ATP-dependent allosteric transitions in CCT. (C) 2008 Elsevier Ltd. All rights reserved.en_US
dc.format.extent469 - 477en_US
dc.languageEnglishen_US
dc.language.isoEnglishen_US
dc.publisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTDen_US
dc.titleATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growthen_US
dc.typeJournal Article
rioxxterms.versionofrecord10.1016/j.jmb.2008.01.011en_US
rioxxterms.licenseref.startdate2008-03-21en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfJOURNAL OF MOLECULAR BIOLOGYen_US
pubs.notesaffiliation: Willison, KR (Reprint Author), Inst Canc Res, Chester Beatty Labs, Canc Res UK, Ctr Cell & Mol Biol, London SW3 6JB, England. Hynes, Gillian M.; McCormack, Elizabeth A.; Willison, Keith R., Inst Canc Res, Chester Beatty Labs, Canc Res UK, Ctr Cell & Mol Biol, London SW3 6JB, England. Shimon, Liat; Horovitz, Amnon, Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel. keywords: CCT; TCP-1; chaperonins; allostery; protein folding keywords-plus: TRANSIENT KINETIC-ANALYSIS; TUMOR-SUPPRESSOR COMPLEX; CYTOPLASMIC CHAPERONIN; IN-VIVO; ACTIN; MECHANISM; PROTEIN; GROEL; TCP-1; COOPERATIVITY research-areas: Biochemistry & Molecular Biology web-of-science-categories: Biochemistry & Molecular Biology author-email: Keith.Willison@icr.ac.uk Amnon.Horovitz@weizmann.ac.il funding-acknowledgement: Cancer Research UK number-of-cited-references: 31 times-cited: 36 usage-count-last-180-days: 0 usage-count-since-2013: 4 journal-iso: J. Mol. Biol. doc-delivery-number: 282RY unique-id: ISI:000254586100014 da: 2018-08-30en_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.volume377en_US
pubs.embargo.termsNot knownen_US
icr.researchteamChromatin Regulationen_US
dc.contributor.icrauthorHynes, Gillianen_US
dc.contributor.icrauthorWillison, Keithen_US


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