Abstract
The selC gene from E. coli codes for a tRNA species (tRNA(UCASer] which is aminoacylated with L-serine and which cotranslationally inserts selenocysteine into selenoproteins. By means of Southern hybridization it was demonstrated that this gene occurs in all enterobacteria tested. To assess whether the unique primary and secondary structural features of the E. coli selC gene product are conserved in that of other organisms, the selC homologue from Proteus vulgaris was cloned and sequenced. It was found that the Proteus selC gene differs from the E. coli counterpart in only six nucleotides, that it displays the same unique properties and that it is expressed and functions in E. coli. This indicates that the unique mechanism of selenocysteine incorporation is not restricted to E. coli but has been conserved as a uniform biochemical process.