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dc.contributor.authorDekker, C
dc.contributor.authorWillison, KR
dc.contributor.authorTaylor, WR
dc.date.accessioned2018-08-13T14:41:17Z
dc.date.issued2011-04
dc.identifier4
dc.identifier.citationPROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2011, 79 pp. 1172 - 1192
dc.identifier.issn0887-3585
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2330
dc.identifier.doi10.1002/prot.22952
dc.description.abstractAn analysis of the apical domain of the Group-I and Group-II chaperonins shows that they have structural similarities to two different protein folds: a “swivel-domain” phosphotransferase and a thioredoxin-like peroxiredoxin. There is no significant sequence similarity that supports either similarity and the degree of similarity based on structure is comparable but weak for both relationships. Based on possible evolutionary transitions, we deduced that a phosphotransferase origin would require both a large insertion and deletion of structure whereas a peroxiredoxin origin requires only a peripheral rearrangement, similar to an internal domain-swap. We postulate that this change could have been triggered by the insertion of a peroxiredoxin into the ATPase domain that led to the modern chaperonin domain arrangement. The peroxidoxin fold is the most highly embellished member of the thioredoxin super-family and the insertion event may have “overloaded” the core, leading to a rearrangement. A peroxiredoxin origin for the domain also provides a functional explanation, as the peroxiredoxins can act as chaperones when they adopt a multimeric ring complex, similar to the chaperonin subunit configuration. In addition, several of the GroEL apical domain hydrophobic residues which interact with the unfolded protein are located in a position that corresponds to the protein substrate binding region of the peroxiredoxin fold. We suggest that the origin of the ur-chaperonin from a thioredoxin/peroxiredoxin fold might also account for the number of thioredoxin-fold containing proteins that interact with chaperonins, such as tubulin and phosducin-like proteins.
dc.format.extent1172 - 1192
dc.languageeng
dc.language.isoeng
dc.publisherWILEY-BLACKWELL
dc.titleOn the evolutionary origin of the chaperonins
dc.typeJournal Article
rioxxterms.versionofrecord10.1002/prot.22952
rioxxterms.licenseref.startdate2011-04
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfPROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
pubs.notesaffiliation: Taylor, WR (Reprint Author), Natl Inst Med Res, MRC, Div Math Biol, Mill Hill, London NW7 1AA, England. Taylor, William R., Natl Inst Med Res, MRC, Div Math Biol, London NW7 1AA, England. Dekker, Carien; Willison, Keith R., Inst Canc Res, Chester Beatty Labs, Sect Cell & Mol Biol, London SW3 6JB, England. keywords: protein folding; molecular chaperones; oxidative stress keywords-plus: CYTOSOLIC CHAPERONIN; CRYSTAL-STRUCTURE; STRUCTURAL CLASSIFICATION; PROTEIN; CCT; GROEL; PEROXIREDOXINS; SEQUENCES; HOMOLOG; COMPLEX research-areas: Biochemistry & Molecular Biology; Biophysics web-of-science-categories: Biochemistry & Molecular Biology; Biophysics author-email: [email protected] number-of-cited-references: 44 times-cited: 18 usage-count-last-180-days: 0 usage-count-since-2013: 16 journal-iso: Proteins doc-delivery-number: 731VY unique-id: ISI:000288138700012 da: 2018-08-13
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.volume79en_US
pubs.embargo.termsNot known
icr.researchteamChromatin Regulationen_US
dc.contributor.icrauthorWillison, Keithen
dc.contributor.icrauthorDekker, Carienen


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