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Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese.
- Source :
-
Journal of bacteriology [J Bacteriol] 1995 Oct; Vol. 177 (19), pp. 5517-22. - Publication Year :
- 1995
-
Abstract
- A peptide consisting of the 17 N-terminal amino acids of native bovine rhodanese in combination with the chaperone DnaJ specifically inhibits release factor- and stop codon-dependent hydrolysis of N-formylmethionine from N(formyl)-methionyl-tRNA bound with AUG to salt-washed ribosomes. Neither the peptide nor DnaJ by itself causes this inhibition. The N-terminal peptide and DnaJ both singularly and combined do not affect the peptidyltransferase reaction per se. The total amount of rhodanese synthesized in the cell-free coupled transcription-translation system is reduced by the peptide, with concomitant accumulation of full-length enzymatically inactive rhodanese polypeptides on ribosomes. In combination with DnaJ, the N-terminal polypeptide inhibits the termination and release of full-length rhodanese peptides that have accumulated on Escherichia coli ribosomes during the course of uninhibited coupled transcription-translation in the cell-free system. This inhibition appears to involve release factor 2-mediated termination at the UGA termination codon in the coding sequence for rhodanese. It is suggested that the N-terminal peptide inhibits the binding of the release factor to ribosomes. These data appear to provide the first report of differential inhibition of the termination reaction on ribosomes without inhibition of the peptidyltransferase reaction and peptide elongation.
- Subjects :
- Amino Acid Sequence
Animals
Cattle
Cell-Free System
Chloramphenicol O-Acetyltransferase biosynthesis
Codon, Terminator
Escherichia coli Proteins
HSP40 Heat-Shock Proteins
Molecular Sequence Data
Peptide Chain Termination, Translational drug effects
Peptide Fragments chemical synthesis
Peptide Fragments pharmacology
RNA, Transfer, Met metabolism
Ribosomes metabolism
Ricin biosynthesis
Tetrahydrofolate Dehydrogenase biosynthesis
Thiosulfate Sulfurtransferase biosynthesis
Heat-Shock Proteins pharmacology
Molecular Chaperones pharmacology
Peptide Termination Factors physiology
Protein Synthesis Inhibitors pharmacology
Thiosulfate Sulfurtransferase pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9193
- Volume :
- 177
- Issue :
- 19
- Database :
- MEDLINE
- Journal :
- Journal of bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- 7559337
- Full Text :
- https://doi.org/10.1128/jb.177.19.5517-5522.1995