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 in

1986 by the parallel discoveries that the genes encoding the
selenoproteins glutathione peroxidase and bacterial formate
dehydrogenase each contain an in-frame TGA codon within their
coding sequence. We now know that this codon directs the
incorporation of selenium, in the form of selenocysteine, into these
proteins. Working with the bacterial system has led to a rapid
increase in our knowledge of selenocysteine biosynthesis and to the
exciting discovery that this system can now be regarded as an
expansion of the genetic code. The prerequisites for such a definition
are co-translational insertion into the polypeptide chain and the
occurrence of a tRNA molecule which carries selenocysteine. Both of
these criteria are fulfilled and, moreover, tRNASec even has its own
special translation factor which delivers it to the translating
ribosome. It is the aim of this article to review the events leading to
the elucidation of selenocysteine as being the 21st amino acid.

Gene for a novel tRNA species that accepts L-serine and

cotranslationally 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 was

recognized 40 years ago. Selenium is incorporated into several
enzymes and transfer RNA species of both prokaryotic and
eukaryotic origin. In enzymes which contain a selenopolypeptide,
selenium is present as covalently bound selenocysteine which
participates in the catalytic reaction. Sequence analysis of the genes
coding for two selenoproteins, formate dehydrogenase H from
Escherichia coli and glutathione peroxidase from mouse and man,
demonstrated that an in-frame UGA opal nonsense codon directs the
incorporation of selenocysteine. In the case of formate dehydrogenase
incorporation occurs cotranslationally. Recently, we identified four
genes whose products are required for selenocysteine incorporation
in E. coli. We report here that one of these genes codes for a tRNA
species with unique properties. It possesses an anticodon
complementary to UGA and deviates in several positions from
sequences, until now, considered invariant in all tRNA species. This
tRNA is aminoacylated with L-serine by the seryl-tRNA ligase which
also charges cognate tRNASer. Selenocysteine, therefore, is
synthesized from a serine residue bound to a natural suppressor
tRNA which recognizes UGA.

Identification of a novel translation factor necessary for the

incorporation of selenocysteine into protein.

Forchhammer K, Leinfelder W, Böck A. Lehrstuhl für Mikrobiologie

der Universität, München, FRG.

During the biosynthesis of selenoproteins in both prokaryotes and

eukaryotes, selenocysteine is cotranslationally incorporated into the
nascent polypeptide chain through a process directed by a UGA
codon that normally functions as a stop codon. Recently, four genes
have been identified whose products are required for selenocysteine
incorporation in Escherichia coli. One of these genes, selC, codes for
a novel transfer RNA species (tRNAUCA) that accepts serine and
cotranslationally inserts selenocysteine by recognizing the specific
UGA codon. The serine residue attached to this tRNA is converted to
selenocysteine in a reaction dependent on functional selA and selD
gene products. By contrast, the selB gene product (SELB) is not
required until after selenocysteyl-tRNA biosynthesis. Here we present
evidence indicating that SELB is a novel translation factor. The
deduced amino-acid sequence of SELB exhibits extensive homology
with the sequences of the translation initiation factor-2 (IF-2) and
elongation factor Tu (EF-Tu). Furthermore, purified SELB protein
binds guanine nucleotides in a 1:1 molar ratio and specifically
complexes selenocysteyl-tRNAUCA, but does not interact with seryl-
tRNAUCA. Thus, SELB could be an amino acid-specific elongation
factor, replacing EF-Tu in a special translational step.

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