Ribosome Rescue by tmRNA Requires Truncated mRNAs

tmRNA targets ribosomes, stalled either on truncated mRNAs or on mRNAs with slowly read sense or stop codons, tags the newly synthesized peptide chains for degradation and allows for their release by a class-1 release factor. We have studied in vitro how the rate of trans-transfer of a peptide from...

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Bibliographic Details
Published in:Journal of molecular biology 2004-04, Vol.338 (1), p.33-41
Main Authors: Ivanova, Natalia, Pavlov, Michael Y., Felden, Brice, Ehrenberg, Måns
Format: Article
Language:English
Subjects:
Bacterial Physiological Phenomena
Bacterial Physiology
Bacterial Toxins
Bacterial Toxins - metabolism
Biochemistry, Molecular Biology
Escherichia coli Proteins
Escherichia coli Proteins - metabolism
Life Sciences
Protein Biosynthesis
protein synthesis
ribosome
Ribosomes
Ribosomes - metabolism
RNA, Bacterial
RNA, Bacterial - genetics
RNA, Bacterial - metabolism
RNA, Messenger
RNA, Messenger - metabolism
RNA, Transfer
RNA, Transfer - metabolism
tmRNA
trans-translation kinetics
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Summary:tmRNA targets ribosomes, stalled either on truncated mRNAs or on mRNAs with slowly read sense or stop codons, tags the newly synthesized peptide chains for degradation and allows for their release by a class-1 release factor. We have studied in vitro how the rate of trans-transfer of a peptide from the P-site tRNA to tmRNA and the efficiency by which tmRNA competes with peptide release factors depend on the length of the mRNA downstream from the P-site. We show that the rate and efficiency of tmRNA action decrease rapidly with increasing down stream length and approach zero when it exceeds 15 bases. We demonstrate that tmRNA action is strongly stimulated by RelE cleavage of mRNA in the A site. We conclude that tmRNA action in vivo must always be preceded by mRNA truncation, and suggest that cleavage of ribosome bound mRNAs is a common element in different bacterial stress responses.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2004.02.043