Release of (oligo) peptidyl-tRNA from ribosomes by erythromycin A.
نویسندگان
چکیده
Erythromycin A released peptidyl-tRNA in the in vitro polypeptide synthesis system with bacterial components programmed by synthetic polynucleotide. This is consistent with our hypothesis that erythromycin A inhibits translocation by preventing proper situation of oligopeptidyl-tRNA in the donor (D) site on ribosomes.
منابع مشابه
Lincosamide antibiotics stimulate dissociation of peptidyl-tRNA from ribosomes.
At nonpermissive temperatures the peptidyl-tRNA hydrolase of pth(Ts) bacterial mutants is inactivated, and cells accumulate peptidyl-tRNA and die. Doses of erythromycin, lincomycin, or clindamycin that inhibited the growth of antibiotic-hypersensitive DB-11 pth+ cells accelerated the killing of DB-11 pth(Ts) cells at nonpermissive temperatures. Erythromycin and lincomycin also stimulated the ac...
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Growing cultures of mutant Escherichia coli with temperature-senstive peptidyl-tRNA hydrolase were shifted to nonpermissive 4o degrees. There followed a roughly linear increase in a fraction of isolated tRNA (over 50% after 20 min) whose amino acid-accepting activity was masked until treatment with active peptidyl-tRNA hydrolase. The ionophoretic mobility of amino acid label associated with thi...
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Antibiotics were used as probes of ribosome topology and function. Studies of [(14)C]chloramphenicol and [(14)C]erythromycin binding to ribosomes and polyribosomes revealed the following features. The requirement of high K(+) concentration (150 mM) for [(14)C]chloramphenicol binding to NH(4)Cl-washed ribosomes resulted from the washing procedure. Neither native 70S ribosomes nor polyribosomes r...
متن کاملRibosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome.
Peptidyl-tRNA dissociation from ribosomes is an energetically costly but apparently inevitable process that accompanies normal protein synthesis. The drop-off products of these events are hydrolysed by peptidyl-tRNA hydrolase. Mutant selections have been made to identify genes involved in the drop-off of peptidyl-tRNA, using a thermosensitive peptidyl-tRNA hydrolase mutant in Escherichia coli. ...
متن کاملThe mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome.
The macrolide-lincosamide-streptogramin B class (MLS) of antibiotics contains structurally different but functionally similar drugs, that all bind to the 50S ribosomal subunit. It has been suggested that these compounds block the path by which nascent peptides exit the ribosome. We have studied the mechanisms of action of four macrolides (erythromycin, josamycin, spiramycin and telithromycin), ...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 72 7 شماره
صفحات -
تاریخ انتشار 1975