1971
DOI: 10.1073/pnas.68.2.496
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Puromycin-Peptide Bond Formation with Reticulocyte Initiation Factors M 1 and M 2

Abstract: The ability to form a "peptide" bond between various forms of Met-tRNA or Phe-tRNA and puromycin has been studied in the reticulocyte cell-free system. When Met-tRNAF, fMet-tRNAF, or N-acetylPhetRNA are used as substrate at low Mg++ concentration (3 mM), reticulocyte initiation factors M1 and M, (M2A + M2B) are required for puromycin-peptide synthesis. In contrast to bacterial systems, this reaction is also stimulated by the elongation factor Ti. When Met-tRNAM or Phe-tRNA is used as substrate, there is no M-f… Show more

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Cited by 30 publications
(18 citation statements)
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“…No conclusive explanation can, a t present, be offered for this finding which is in agreement with data presented by other authors [5]. One might speculate, however, that in mammalian systems, the triplet associates preferentially with the ribosomal P-site to which Met-tRNAfMet is transferred by the initiation factors [22,30]. I n this case, apparently, the codon would not become available to MettRNAMet transferred to the ribosomal A-site and a stimulating effect of the triplet on the T-factorcatalyzed binding of either Met-tRNAMet should not be observed.…”
Section: Discussionsupporting
confidence: 75%
See 1 more Smart Citation
“…No conclusive explanation can, a t present, be offered for this finding which is in agreement with data presented by other authors [5]. One might speculate, however, that in mammalian systems, the triplet associates preferentially with the ribosomal P-site to which Met-tRNAfMet is transferred by the initiation factors [22,30]. I n this case, apparently, the codon would not become available to MettRNAMet transferred to the ribosomal A-site and a stimulating effect of the triplet on the T-factorcatalyzed binding of either Met-tRNAMet should not be observed.…”
Section: Discussionsupporting
confidence: 75%
“…This result could possibly be explained by the binding of Met-tRNAf Met to both ribosomal sites, with T factor responsible for transferring MettRNAfMet to the A-site and the ribosomal wash fraction bringing the same tRNA species to the peptidy1 site. Alternatively, the additive effects of T factor and ribosomal wash on the binding of MettRNAfMet could reflect an assistant role of T factor in chain initiation similar to the enhancing effect of T factor on the formation of an initiation complex as observed by Shafritz et al in a cell-free system from rabbit reticulocytes [22]. The fact that an additive effect of T factor and ribosomal wash was not found with formylated initiator tRNA seems to favour the first explanation.…”
Section: Binding Experimentsmentioning
confidence: 72%
“…Although it is not yet possible to define the exact role of each M factor in tRNA binding to ribosomes, the present studies, together with other data from this laboratory (2,19,28), suggest that Ml + M2 confer specific recognition of Met-tRNAF species to ribosomes containing endogenous messenger RNA, as well as to ribosomes with artificial template. This recognition appears to take place on the small ribosomal subunit in both the endogenous mRNA system and the artificial AUG-template system.…”
Section: Methodsmentioning
confidence: 65%
“…Fusidic acid and aurintricarboxylic acid were the gifts of H. Weissbach and A. Grollman, respectively. The assays for aminoacyl-tRNA binding, peptide-bond formation with puromycin, and cell-free poly(U)-dependent protein synthesis were also as reported (4,7,8).…”
Section: Methodsmentioning
confidence: 99%
“…The preparation of washed reticulocyte ribosomes, elongation factors T, and T2, initiation factors M1 and M2(AB), and acylated reticulocyte tRNA was as reported (4,(7)(8)(9), except that M1 was purified through phosphocellulose as well as DEAE-cellulose and Sephadex G-150 chromatography. The separation of M2 into two components, M2A (which elutes at the void volume on Sephadex G-200 chromatography) and M2B (which has a molecular weight of 20,000-40,000), will be reported elsewhere.…”
Section: Methodsmentioning
confidence: 99%