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J Biol Chem, Vol. 275, Issue 20, 14846-14852, May 19, 2000
From the The synthesis of eukaryotic selenoproteins
involves the recoding of an internal UGA codon as a site for
selenocysteine incorporation. This recoding event is directed by a
selenocysteine insertion sequence in the 3'-untranslated region.
Because UGA also functions as a signal for peptidyl-tRNA hydrolysis, we
have investigated how the rates of translational termination and
selenocysteine incorporation relate to cis-acting elements
in the mRNA as well as to trans-acting factors in the
cytoplasm. We used cis-elements from the phospholipid
glutathione peroxidase gene as the basis for this work because of its
relatively high efficiency of selenocysteine incorporation. The last
two codons preceding the UGA were found to exert a far greater
influence on selenocysteine incorporation than nucleotides downstream
of it. The efficiency of selenocysteine incorporation was generally
much less than 100% but could be partially enhanced by concomitant
overexpression of the tRNASec gene. The combination of two
or three UGA codons in one reading frame led to a dramatic reduction in
the yield of full-length protein. It is therefore unlikely that
multiple incorporations of selenocysteine are processive with respect
to the mode of action of the ribosomal complex binding to the UGA site.
These observations are discussed in terms of the mechanism of
selenoprotein synthesis and its ability to compete with termination at
UGA codons.
Eukaryotic Selenocysteine Incorporation Follows a Nonprocessive
Mechanism That Competes with Translational Termination*
§,§,,,
Posttranscriptional Control Group,
Department of Biomolecular Sciences, University of Manchester
Institute of Science and Technology, Manchester M60 1QD, United Kingdom
and ¶ Department of Biochemistry, Technische Universität
Braunschweig, Mascheroder Weg 1, D-38124 Braunschweig, Germany
*
This work was supported by the British Biotechnology and
Biological Sciences Research Council and the Wellcome Trust.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed:
Posttranscriptional Control Group, Department of Biomolecular Sciences,
UMIST, P.O. Box 88, Manchester M60 IQD, UK. E-mail:
J.McCarthy@umist.ac.uk.
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