Abstract：
:The trans-translation system in bacteria promotes recycling of stalled ribosomes and targets incomplete peptides for proteolysis. In Escherichia coli, loss of trans-translation function has little effect on growth under normal laboratory conditions. Among the subtle phenotypes of tmRNA-deficient mutants is the inability to plate certain lambda imm(P22) phages. This phenotype is dependent on the ribosome recycling functions of the trans-translation system but is independent of its proteolysis-targeting activity. The experiments described here show that translation of the first (resume) codon of the tmRNA open reading frame by a tRNA is both necessary and sufficient for ribosome recycling. While a variety of sense codons can replace the naturally-occurring GCA alanine codon as the resume codon, both AAA and AAG lysine codons are non-functional resume codons. These results suggest that the main function of tmRNA in releasing stalled ribosomes is to supply a stop codon and so facilitate termination and subsequent ribosome recycling.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
O'Connor Mdoi
10.1016/j.bbrc.2007.03.142subject
Has Abstractpub_date
2007-05-25 00:00:00pages
276-81issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(07)00634-1journal_volume
357pub_type
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journal_title：Biochemical and biophysical research communications
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journal_title：Biochemical and biophysical research communications
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