Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Peptide Chain Initiation, Translational”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1973

Protein synthesis.

Explore the source record for details and available documents.

Peptide Biosynthesis↗
PubMed1981

The ribosome.

Explore the source record for details and available documents.

Animals↗
PubMed1978

Inhibition of globin synthesis by rabbit reticulocyte rRNAs.

The effect of concentration of rabbit reticulocyte rRNAs on the translation of rabbit globin mRNAs was studied by using a rabbit reticulocyte lysate system. Globin synthesis was studied using L-[U-14C]leucine. Both the 18S and 28S rRNA inhibited globin synthesis. The 18S rRNA inhibited the synthesis of alpha-globin chain more than that of beta chain, but the 28S rRNA inhibited the synthesis of alpha- and beta-chains almost equally. Nascent chains prelabelled with [14C]Leu or f[35S]Met were released at various concentrations of rRNAs. Release of the nascent chains was not inhibited at various concentrations of rRNAs. The ratios [14C]alpha/[14C]beta and [35S]alpha/[35S]beta in the released chains were almost constant at various concentrations of rRNAs. It therefore appears that the inhibition of globin synthesis by these rRNAs was at the step of initiation.

Animals↗
PubMed1975

Inhibition of protein synthesis in intact HeLa cells.

Polysome analysis has proved to be a sensitive probe for the mode of action of inhibitors of protein synthesis in intact HeLa cells. To classify the active compounds as inhibitors of initiation, elongation, or termination, their effects on the cellular polyribosome pattern were compared under three conditions. These conditions tested (i) their direct effect on the polyribosome profile; (ii) their effect on ribosome run-off produced by hypertonicity; and (iii) their effects on recovery from hypertonicity. Using this technique, diacetoxyscirpenol, 2-(4-methyl-2,6-dinitroanilino)-N-methylpropionamide, and three alkaloids, harringtonine, isoharringtonine, and homoharringtonine, were found to be inhibitors of initiation. Polysome analysis indicated that in HeLa cells 7.8 x 10(-7) M pactamycin, which inhibited protein synthesis 94%, interfered with elongation as well as initiation under these conditions. Emetine, anisomycin, cycloheximide, and trichodermin each gave polysome patterns consistent with inhibition of elongation. Fusidic acid and aurintricarboxylic acid inhibited incorporation of [(14)C]leucine into intact HeLa cells, but polysome analysis did not localize any specific inhibitory effects to the initiation, elongation, or termination steps of protein synthesis. The use of specific inhibitors of initiation of protein synthesis has indicated that most, if not all, mammalian messenger ribonucleic acids contain a single initiation site.

Amino Acids↗
PubMed1987

Bovine mitochondrial ribosomes: effect of cations and heterologous dissociation factors on subunit interactions.

The effects of cations and ribosome dissociation factors on the equilibrium between the bovine mitochondrial ribosome and its subunits has been investigated. As observed with other ribosomes, Mg2+ ions promote subunit association while monovalent cations promote subunit dissociation. E. coli IF-3 will prevent the reassociation of mitochondrial 28 S and 39 S subunits. However, at least 5-fold higher concentrations of IF-3 are required with mitochondrial subunits than are required with bacterial subunits. The cytoplasmic factor eIF-6, has no detectable activity in preventing mitochondrial ribosomal subunit association.

Cations↗