A functional peptidyl - tRNA hydrolase
نویسندگان
چکیده
Ricarda Richter, Joanna Rorbach, Aleksandra Pajak, Paul M Smith, Hans J Wessels, Martijn A Huynen, Jan A Smeitink, Robert N Lightowlers* and Zofia M Chrzanowska-Lightowlers* Mitochondrial Research Group, Institute for Ageing and Health, Medical School, Newcastle University, Newcastle upon Tyne, UK, Nijmegen Centre for Mitochondrial Disorders, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands and Center for Molecular and Biomolecular Informatics, NCMLS, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands
منابع مشابه
Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase.
Peptidyl-tRNA hydrolase activity from Escherichia coli ensures the recycling of peptidyl-tRNAs produced through abortion of translation. This activity, which is essential for cell viability, is carried out by a monomeric protein of 193 residues. The structure of crystalline peptidyl-tRNA hydrolase could be solved at 1.2 A resolution. It indicates a single alpha/beta globular domain built around...
متن کاملPeptidyl transfer RNA dissociates during protein synthesis from ribosomes of Escherichia coli.
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...
متن کاملPeptidyl-tRNA hydrolase and its critical role in protein biosynthesis.
Peptidyl-tRNA hydrolase (Pth) releases tRNA from peptidyl-tRNA by cleaving the ester bond between the peptide and the tRNA. Genetic analyses using Escherichia coli harbouring temperature-sensitive Pth have identified a number of translation factors involved in peptidyl-tRNA release. Accumulation of peptidyl-tRNA in the cells leads to depletion of aminoacyl-tRNA pools and halts protein biosynthe...
متن کاملLincosamide 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...
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 کاملSequestration of specific tRNA species cognate to the last sense codon of an overproduced gratuitous protein.
High-level expression of non-functional model proteins, derived from elongation factor EF-Tu by the deletion of an essential domain, greatly inhibits the growth of Escherichia coli partly deficient in peptidyl-tRNA hydrolase. High-level expression in wild-type cells has little effect on growth. The inhibitory effect is therefore presumably due to the sequestration of essential tRNA species, par...
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تاریخ انتشار 2010