Abstract
Methanococcus maripaludis possesses two sets of F420-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.
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Böck, A., Rother, M. A pseudo-SECIS element in Methanococcus voltae documents evolution of a selenoprotein into a sulphur-containing homologue. Arch Microbiol 183, 148–150 (2005). https://doi.org/10.1007/s00203-004-0744-7
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DOI: https://doi.org/10.1007/s00203-004-0744-7