{"refrec":{"BRefID":280815,"RR":"<b>Dufernez, F.; Derelle, E.; Noël, C.; Sanciu, G.; Mantini, C.; Dive, D.; Soyer-Gobillard, M.-O.; Capron, M.; Pierce, R.J.; Wintjens, R.; Guillebault, D.; Viscogliosi, E.</b> (2008). Molecular characterization of iron-containing superoxide dismutases in the heterotrophic dinoflagellate <i>Crypthecodinium cohnii</i>. <i>Protist 159(2)</i>: 223-238. <a href=\"https://dx.doi.org/10.1016/j.protis.2007.11.005\" target=\"_blank\">https://dx.doi.org/10.1016/j.protis.2007.11.005</a>","BEntID":272834,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Protist 159(2)</i>: 223-238. <a href=\"https://dx.doi.org/10.1016/j.protis.2007.11.005\" target=\"_blank\">https://dx.doi.org/10.1016/j.protis.2007.11.005</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Dufernez, F.; Derelle, E.; Noël, C.; Sanciu, G.; Mantini, C.; Dive, D.; Soyer-Gobillard, M.-O.; Capron, M.; Pierce, R.J.; Wintjens, R.; Guillebault, D.; Viscogliosi, E.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Dufernez, F. <i>et al.</i>","Englishabstract":"Superoxide dismutases (SODs) are a family of antioxidant enzymes that catalyse the degradation of toxic superoxide radicals in obligate and facultative aerobic organisms. Here, we report the presence of a multi-copy gene family encoding SODs in the heterotrophic dinoflagellate <i>Crypthecodinium cohnii</i>. All the genes identified (<i>sod1</i> to <i>sod17</i>) have been cloned and sequenced, and shown to encode potentially functional dimeric iron-containing SOD isozymes. Our data revealed a considerable molecular heterogeneity of this enzyme in <i>C. cohnii</i> at both genomic and transcriptional levels. The <i>C. cohnii</i> SOD1, overexpressed in <i>Escherichia coli</i>, was active and its structure obtained by homology modeling using X-ray crystal structures of homologues exhibited the typical fold of dimeric FeSODs. Phylogenetic studies including 110 other dimeric FeSODs and closely related cambialistic dimeric SOD sequences showed that the <i>C. cohnii</i> SODs form a monophyletic group and have all been acquired by the same event of horizontal gene transfer. It also revealed a dichotomy within the <i>C. cohnii</i> SOD sequences that could be explained by an ancestral <i>sod</i> gene duplication followed by subsequent gene duplications within each of the two groups. Enzyme assays of SOD activity indicated the presence of two FeSOD activities in <i>C. cohnii</i> cell lysate whereas MnSOD and Cu/ZnSOD were not detected. These activities contrasted with the SOD repertoire previously characterized in photosynthetic dinoflagellates. To explain these differences, a hypothetical evolutionary scenario is proposed that suggests gains and losses of <i>sod</i> genes in dinoflagellates.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Molecular characterization of iron-containing superoxide dismutases in the heterotrophic dinoflagellate <i>Crypthecodinium cohnii</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"antioxidant enzymes; Crypthecodinium; dinoflagellates; evolution;multigene family; phylogeny; superoxide dismutase","OtherDescriptors":null,"Notes":null,"AnaPub":2008,"MonPub":null,"DateUpdate":"2022-07-12","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000255122000005","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.protis.2007.11.005"},"refs":null,"anarec":{"AnaID":280815,"PubliDate":2008,"Pagination":"223-238","XtraPublOfAnaID":null,"ISBN":null,"Volume":"159","Issue":"2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":45701,"SerRR":"Protist. 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