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dc.contributor.authorLe, Dung Tien
dc.contributor.authorLee, Byung Cheon
dc.contributor.authorMarino, Stefano M.
dc.contributor.authorZhang, Yan
dc.contributor.authorFomenko, Dmitri E.
dc.contributor.authorKaya, Alaattin
dc.contributor.authorHacıoğlu, Elise
dc.contributor.authorKwak, Geun-Hee
dc.contributor.authorKoç, Ahmet
dc.contributor.authorKim, Hwa-Young
dc.contributor.authorGladyshev, Vadim N.
dc.date.accessioned2017-01-25T12:22:03Z
dc.date.available2017-01-25T12:22:03Z
dc.date.issued2009-02
dc.identifier.citationLe, D. T., Lee, B. C., Marino, S. M., Zhang, Y., Fomenko, D. E., Kaya, A., Hacıoğlu, E., Kwak, G. H., Koç, A., Kim, H. Y. and Gladyshev, V. N. (2009). Functional analysis of free methionine-R-sulfoxide reductase from saccharomyces cerevisiae. Journal of Biological Chemistry, 248(7), 4354-4364. doi:10.1074/jbc.M805891200en_US
dc.identifier.issn0021-9258
dc.identifier.urihttp://dx.doi.org/10.1074/jbc.M805891200
dc.identifier.urihttp://hdl.handle.net/11147/2857
dc.description.abstractMethionine sulfoxide reductases (Msrs) are oxidoreductases that catalyze thiol-dependent reduction of oxidized methionines. MsrA and MsrB are the best known Msrs that repair methionine S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO) residues in proteins, respectively. In addition, an Escherichia coli enzyme specific for free Met-R-SO, designated fRMsr, was recently discovered. In this work, we carried out comparative genomic and experimental analyses to examine occurrence, evolution, and function of fRMsr. This protein is present in single copies and two mutually exclusive subtypes in about half of prokaryotes and unicellular eukaryotes but is missing in higher plants and animals. A Saccharomyces cerevisiae fRMsr homolog was found to reduce free Met-R-SO but not free Met-S-SO or dabsyl-Met-R-SO. fRMsr was responsible for growth of yeast cells on Met-R-SO, and the double fRMsr/MsrA mutant could not grow on a mixture of methionine sulfoxides. However, in the presence of methionine, even the triple fRMsr/MsrA/MsrB mutant was viable. In addition, fRMsr deletion strain showed an increased sensitivity to oxidative stress and a decreased life span, whereas overexpression of fRMsr conferred higher resistance to oxidants. Molecular modeling and cysteine residue targeting by thioredoxin pointed to Cys101 as catalytic and Cys125 as resolving residues in yeast fRMsr. These residues as well as a third Cys, resolving Cys91, clustered in the structure, and each was required for the catalytic activity of the enzyme. The data show that fRMsr is the main enzyme responsible for the reduction of free Met-R-SO in S. cerevisiae.en_US
dc.language.isoengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.relation.isversionof10.1074/jbc.M805891200en_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCatalytic activityen_US
dc.subjectSaccharomyces cerevisiaeen_US
dc.subjectMethionine sulfoxideen_US
dc.subjectMethionine sulfoxide reductaseen_US
dc.subjectYeast cellen_US
dc.subjectEnzyme activityen_US
dc.titleFunctional analysis of free methionine-R-sulfoxide reductase from saccharomyces cerevisiaeen_US
dc.typearticleen_US
dc.contributor.authorIDTR110769en_US
dc.contributor.iztechauthorHacıoğlu, Elise
dc.contributor.iztechauthorKoç, Ahmet
dc.relation.journalJournal of Biological Chemistryen_US
dc.contributor.departmentİYTE, Fen Fakültesi, Moleküler Biyoloji ve Genetik Bölümüen_US
dc.identifier.volume248en_US
dc.identifier.issue7en_US
dc.identifier.startpage4354en_US
dc.identifier.endpage4364en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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