Nucleic Acids Research, Vol 25, Issue 12 2254-2258, Copyright © 1997 by Oxford University Press
G Drugeon, O Jean-Jean, L Frolova, X Le Goff, M Philippe, L Kisselev and AL Haenni
It is known from experiments with bacteria and eukaryotic viruses that
readthrough of termination codons located within the open reading frame
(ORF) of mRNAs depends on the availability of suppressor tRNA(s) and the
efficiency of termination in cells. Consequently, the yield of readthrough
products can be used as a measure of the activity of polypeptide chain
release factor(s) (RF), key components of the translation termination
machinery. Readthrough of the UAG codon located at the end of the ORF
encoding the coat protein of beet necrotic yellow vein furovirus is
required for virus replication. Constructs harbouring this suppressible UAG
codon and derivatives containing a UGA or UAA codon in place of the UAG
codon have been used in translation experiments in vitro in the absence or
presence of human suppressor tRNAs. Readthrough can be virtually abolished
by addition of bacterially-expressed eukaryotic RF1 (eRF1). Thus, eRF1 is
functional towards all three termination codons located in a natural mRNA
and efficiently competes in vitro with endogenous and exogenous suppressor
tRNA(s) at the ribosomal A site. These results are consistent with a
crucial role of eRF1 in translation termination and forms the essence of an
in vitro assay for RF activity based on the abolishment of readthrough by
eRF1.
ARTICLES
Eukaryotic release factor 1 (eRF1) abolishes readthrough and competes with suppressor tRNAs at all three termination codons in messenger RNA
Institut Jacques Monod, 2 Place Jussieu-Tour 43, 75251 Paris Cedex 05, France.
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