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Background  Deleterious phenomena of protein oxidation affect every aerobic organism and methionine residues are their elective targets. The reduction of methionine sulfoxides back to methionines is catalyzed by methionine-sulfoxide reductases (Msrs), enzymes which are particularly active in microorganisms because of their unique nature of individual cells directly exposed to environmental oxidation.    Results  From the transcriptionally active somatic genome of a common free-living marine protist ciliate,  Euplotes raikovi , we cloned multiple gene isoforms encoding Msr of type A (MsrA) committed to repair methionine-S-sulfoxides. One of these isoforms, in addition to including a MsrA-specific nucleotide sequence, included also a sequence specific for a Msr of type B (MsrB) committed to repair methionine-R-sulfoxides. Analyzed for its structural relationships with MsrA and MsrB coding sequences of other organisms, the coding region of this gene (named  msrAB ) showed much more significant relationships with Msr gene coding sequences of Rhodobacterales and Rhizobiales (Alphaproteobacteria), than of other eukaryotic organisms.    Conclusions  Based on the fact that the  msrAB  gene is delimited by  Euplotes -specific regulatory 5′ and 3′ regions and telomeric C 4 A 4 /G 4 T 4  repeats, it was concluded that  E. raikovi  inherited the coding region of this gene through a phenomenon of horizontal gene transfer from species of Alphaproteobacteria with which it coexists in nature and on which it likely feeds.    Electronic supplementary material  The online version of this article (doi:10.1186/s12866-014-0288-1) contains supplementary material, which is available to authorized users.

bmc microbiology

Evidence for methionine-sulfoxide-reductase gene transfer from Alphaproteobacteria to the transcriptionally active (macro)nucleus of the ciliate, Euplotes raikovi