A pseudo-SECIS element in Methanococcus voltae documents evolution of a selenoprotein into a sulphur-containing homologue.
Methanococcus maripaludis possesses two sets of F(420)-non-reducing hydrogenases which are differentially expressed in response to the selenium content of the medium. One of the subunits of the selenium-containing hydrogenase, VhuD, contains two selenocysteine residues, whereas the homologue of M. voltae possesses cysteine residues in the equivalent positions. Analysis of the 3' non-translated region of the M. voltae vhuD mRNA revealed the existence of a structure resembling the consensus of archaeal SECIS elements but with deviations rendering it non-functional in determining selenocysteine insertion. The presence of a pseudo-SECIS element in the 3' non-translated region of the vhuD mRNA from M. voltae suggests that VhuD from this organism has developed from a selenocysteine-containing ancestor. The 3' non-translated region from the VhcD homologues neither contained a SECIS nor a pseudo SECIS element.
Böck
August
A
Department I, Faculty of Biology, University of Munich, Maria Ward Strasse 1a, 80638 Munich, Germany. august.boeck@lrz.uni-muenchen.de
Rother
Michael
M
D020413:3' Untranslated Regions / Q000737:chemistry*; D019843:Archaeal Proteins / Q000235:genetics*; D001483:Base Sequence; D006864:Hydrogenase / Q000235:genetics*; D017017:Methanococcus / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics*; D019642:RNA, Archaeal / Q000737:chemistry*; D051140:Selenoproteins
D020413:3' Untranslated Regions; D019843:Archaeal Proteins; D011506:Proteins; D019642:RNA, Archaeal; D051140:Selenoproteins; D006864:Hydrogenase