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dc.contributor.authorConway de Macario, E.
dc.contributor.authorRobb, F.T.
dc.contributor.authorMacario, A.J.L.
dc.date.accessioned2019-07-15T16:16:58Z
dc.date.available2019-07-15T16:16:58Z
dc.date.issued2017
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85031001940&doi=10.3389%2ffmolb.2016.00084&partnerID=40&md5=71b15d693dfef304772d5f874e54d1cb
dc.identifier.urihttp://hdl.handle.net/10713/10026
dc.description.abstractAll archaea have a chaperonin of Group II (thermosome) in their cytoplasm and some have also a chaperonin of Group I (GroEL; Cpn60; Hsp60). Conversely, all bacteria have GroEL, some in various copies, but only a few have, in addition, a chaperonin (tentatively designated Group III chaperonin) very similar to that occurring in all archaea, i.e., the thermosome subunit, and in the cytosol of eukaryotic cells, named CCT. Thus, nature offers a range of prokaryotic organisms that are potentially useful as experimental models to study the human CCT and its abnormalities. This is important because many diseases, the chaperonopathies, have been identified in which abnormal chaperones, including mutant CCT, are determinant etiologic-pathogenic factors and, therefore, research is needed to elucidate their pathologic features at the molecular level. Such research should lead to the clarification of the molecular mechanisms underlying the pathologic lesions observed in the tissues and organs of patients with chaperonopathies. Information on these key issues is necessary to make progress in diagnosis and treatment. Some of the archaeal organisms as well as some of the bacterial models suitable for studying molecular aspects pertinent to human mutant chaperones are discussed here, focusing on CCT. Results obtained with the archaeon Pyrococcus furiosus model to investigate the impact of a pathogenic CCT5 mutation on molecular properties and chaperoning functions are reviewed. The pathogenic mutation examined weakens the ability of the chaperonin subunit to form stable hexadecamers and as a consequence, the chaperoning functions of the complex are impaired. The future prospect is to find means for stabilizing the hexadecamer, which should lead to a recovering of chaperone function and the improving of lesions and clinical condition. Copyright 2017 Conway de Macario, Robb and Macario.en_US
dc.description.urihttps://www.doi.org/10.3389/fmolb.2016.00084en_US
dc.language.isoen_USen_US
dc.publisherFrontiers Media S.A.en_US
dc.relation.ispartofFrontiers in Molecular Biosciences
dc.subjectArchaeaen_US
dc.subjectCCT-like chaperonin in bacteriaen_US
dc.subjectCCT5 mutationsen_US
dc.subjectChaperonopathiesen_US
dc.subjectExperimental modelsen_US
dc.subjectGroup II chaperoninsen_US
dc.subjectHexadecamer instabilityen_US
dc.subjectPyrococcus furiosusen_US
dc.titleProkaryotic chaperonins as experimental models for elucidating structure-function abnormalities of human pathogenic mutant counterpartsen_US
dc.typeArticleen_US
dc.identifier.doi10.3389/fmolb.2016.00084


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