Selenocysteine: the 21st amino acid
.See its structure
Böck A,Forchhammer K,Heider J,Leinfelder W,Sawers G,Veprek B,Zinoni
F.Lehrstuhl für Mikrobiologie, Universität München, Germany.
Great excitement was elicited in the field of selenium biochemistry in1986 by the parallel discoveries that the genes encoding theselenoproteins glutathione peroxidase and bacterial formatedehydrogenase each contain an in-frame TGA codon within theircoding sequence. We now know that this codon directs theincorporation of selenium, in the form of selenocysteine, into theseproteins. Working with the bacterial system has led to a rapidincrease in our knowledge of selenocysteine biosynthesis and to theexciting discovery that this system can now be regarded as anexpansion of the genetic code. The prerequisites for such a definitionare co-translational insertion into the polypeptide chain and theoccurrence of a tRNA molecule which carries selenocysteine. Both of these criteria are fulfilled and, moreover, tRNASec even has its ownspecial translation factor which delivers it to the translatingribosome. It is the aimof this article toreviewthe events leading to
the elucidation of selenocysteine as being the 21st amino acid.
Gene for a novel tRNA species that accepts L-serine andcotranslationally inserts selenocysteine.
Leinfelder W,Zehelein E,Mandrand-Berthelot MA,Böck A. Institut für Genetik und
Mikrobiologie, Universität München, FRG.
The biological requirement of the trace element selenium wasrecognized 40 years ago. Selenium is incorporated into severalenzymes and transfer RNA species of both prokaryotic andeukaryotic origin. In enzymes which contain a selenopolypeptide,selenium is present as covalently bound selenocysteine whichparticipates in the catalytic reaction. Sequence analysis of the genescoding for two selenoproteins, formate dehydrogenase H fromEscherichia coli and glutathione peroxidase from mouse and man,demonstrated that an in-frame UGA opal nonsense codon directs theincorporation of selenocysteine. In the case of formate dehydrogenaseincorporation occurs cotranslationally. Recently, we identified fourgenes whose products are required forselenocysteine incorporationin E. coli. We report here that one of these genes codes for a tRNAspecies with unique properties. It possesses an anticodoncomplementary to UGA and deviates in several positions fromsequences, until now, considered invariant in all tRNA species. This
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