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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/21128
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dc.contributor.authorFoltopoulou, P. F.en
dc.contributor.authorZachariadis, G. A.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorTsiftsoglou, A. S.en
dc.contributor.authorPapadopoulou, L. C.en
dc.date.accessioned2015-11-24T19:12:53Z-
dc.date.available2015-11-24T19:12:53Z-
dc.identifier.issn1096-7192-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21128-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectCarrier Proteinsen
dc.subjectCation Transport Proteins/*metabolismen
dc.subjectCircular Dichroismen
dc.subjectCopper/*metabolismen
dc.subjectDimerizationen
dc.subjectHumansen
dc.subjectMitochondria/*metabolismen
dc.subjectMitochondrial Proteinsen
dc.subjectModels, Molecularen
dc.subjectMolecular Sequence Dataen
dc.subject*Mutationen
dc.subjectProtein Bindingen
dc.subjectProtein Conformationen
dc.subjectProteins/genetics/*metabolismen
dc.subjectRecombinant Proteins/genetics/metabolismen
dc.titleHuman recombinant mutated forms of the mitochondrial COX assembly Sco2 protein differ from wild-type in physical state and copper binding capacityen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1016/j.ymgme.2003.11.006-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/14972329-
heal.identifier.secondaryhttp://ac.els-cdn.com/S1096719203002610/1-s2.0-S1096719203002610-main.pdf?_tid=e05f3c8ff97e473459db5a4cfb406c5a&acdnat=1333004718_1b827757c041d44d443daf79152de02f-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2004-
heal.abstractThe human Sco2 protein is a cytochrome c oxidase assembly protein that participates in mitochondrial copper pathway, acting downstream of Cox17 protein. In a previous work, we detected mutations in the human SCO2 gene in three unrelated infants with fatal cardioencephalomyopathy and COX deficiency. In this study, full-length processed recombinant wild-type and two mutated forms of hSco2p (w/t-rhSco2p, E140K-rhSco2p, and S225F-rhSco2p) were produced in bacteria as soluble recombinant peptides for the first time and evaluated for differences in their physical state and ability to bind copper. Our data indicate the following: (a) w/t-rhSco2p and S225F-rhSco2p were found to be in a monomeric form in contrast to E140K-rhSco2p that was in a major non-reducible dimer and a minor monomer form; (b) wild-type and mutated rhSco2p exhibited clear differences in their physical conformational state, as shown by circular dichroism and thermal denaturation analyses; (c) copper binding studies showed that E140K-rhSco2p bound markedly less copper while S225F-rhSco2p more than expected as compared to amount of the copper bound with w/t-rhSco2p. rhCox17p served as positive control experiment. These data indicate that S225F and E140K mutations found in the SCO2 gene derived from patients alter the physical conformational state of encoded hSco2p that may disturb the normal copper transport pathway in mitochondria. These findings are valuable for understanding the molecular basis of fatal cardioencephalomyopathy and COX deficiency and for designing appropriate pharmacological interventions.en
heal.journalNameMol Genet Metaben
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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