Catalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coli

Monro, R.E.

doi:10.1016/0022-2836(67)90271-9

Cited by 266 publications

(67 citation statements)

References 7 publications

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“…This peptide bond formation has been attributed to the fact that in E. coli the peptidyl transferase seems to be a ribosomal protein [27]. The small amount of peptide formed using yeast ribosomes (Fig.…”

Section: Discussionmentioning

confidence: 96%

Guanosine Triphosphate Dependent Enzymic Binding of Aminoacyl Transfer Ribonucleic Acid to Yeast Ribosomes

Ayuso

Heredia

1968

European Journal of Biochemistry

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The binding of phenylalanyl-tRNA to purified yeast ribosomes at low magnesium concentrations is dependent upon one of the yeast supernatant transfer factors (factor A). This reaction requires GTP. The GTP analogue guanylyl methylene diphosphonate cannot be substituted for GTP but it acts as a good inhibitor. After incubation of the ribosomes with phenylalanyl-tRNA, factor A and GTP practically no compound other than phenylalanyl-tRNA itself is found linked to the ribosomes.I n addition to this enzymic type of binding, phenylalanyl-tRNA is also bound to yeast ribosomes in the absence offactor A and GTP provided that the magnesium concentration is increased to about 20 mM. This non-enzymic binding is effectively inhibited by deacylated tRNA and this inhibition is prevented if factor A and GTP are included in the incubation mixtures.The binding of N-acetylphenylalanyl-tRNA to yeast ribosomes also requires GTP, and is dependent upon factor(s) other than the amino acid transfer factors, which are bound t o the ribosomes.Evidence obtained with an Escherichia coli system has shown that the binding of the initiator N-formylmethionyl-tRNA to the ribosome-template complex is mediated by initiation factors in a reaction which requires GTP [I-61. Whether the binding of the aminoacyl-tRNAs involved in the elongation of the peptide chain is enzymically mediated or not has been a point of discussion during the last few years. Schweet and his group fist reported that the binding of phenylalanyl-tRNA to rabbit reticulocytes ribosomes requires one of the amino acid transfer factors (TF,) and GTP [7]. A number of efforts to show this dependence with other systems were unsuccessful. While this work was in progress it has been reported that the binding of non initiator aminoacyl-tRNAs to E. coli [8,9] and rat liver [lo] ribosomes is also mediated by one of the amino acid transfer factors in a GTP dependent reaction.I n a previous paper we reported that 'yeast ribosomes can effectively bind phenylalanyl-tRNA a t high magnesium concentrations in the absence of supernatant transfer factors and GTP [ll]. After the resolution of the yeast amino acid transfer system into complementary factors [12-141 we made further efforts to elucidate the role of these transfer factors in amino acid polymerization. We have now found U n w l abbreviations. PPO, 2,5 diphenyloxazole; POPOP, 1,4-bis-2-(5-phenyl-oxazolyl)benzene; GMP-PCP, 5'-guanylyl-p y -methyhe diphosphonate, tRNA, transfer RNA, phenylalanyl-tRNA, charged tRNA carrying phenylalanyl residue. that a t magnesium concentrations within the physiological range the poly U directed binding of phenylalanyl-tRNA t o yeast ribosomes is dependent on one of the yeast amino acid transfer factors and GTP. I n contrast with these findings, neither of the amino acid transfer factors are involved in the binding of N-acetylphenylalanyl-tRNA to yeast ribosomes. Our results suggest that N-acetylphenylalanyl-tRNA is bound to yeast ribosomes through the action of some other factor(s), presumably initiation fact...

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Section: Discussionmentioning

confidence: 96%

Guanosine Triphosphate Dependent Enzymic Binding of Aminoacyl Transfer Ribonucleic Acid to Yeast Ribosomes

Ayuso

Heredia

1968

European Journal of Biochemistry

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“…The effect of Evn on the peptidyl transferase activity was analyzed by using 70S ribosomes in a ''standard'' peptidyl transferase assay (22) or ''fragment reaction'' catalyzed by isolated large ribosomal subunits (23).…”

Section: Methodsmentioning

confidence: 99%

A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit

Belova¹,

Tenson²,

Xiong³

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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“…The nascent peptide is transfered from tRNA bound at the P site on to amino acyl-tRNA bound at an adjacent A site [2]. This reaction requires an enzyme, peptidyl transferase, which is an integral part of the 50 S subunit [3] . Before the peptide chain can elongate further, peptidyl-tRNA bound at site A must be translocated to site P to allow a further amino acyl-tRNA to attach at site A. Translocation requires GTP hydrolysis and 'G' factor [4].…”

Section: Introductionmentioning

confidence: 99%

Modes of action of erythromycin and thiostrepton as inhibitors of protein synthesis

Cannon¹,

Burns²

1971

FEBS Letters

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Catalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coli

Cited by 266 publications

References 7 publications

Guanosine Triphosphate Dependent Enzymic Binding of Aminoacyl Transfer Ribonucleic Acid to Yeast Ribosomes

Guanosine Triphosphate Dependent Enzymic Binding of Aminoacyl Transfer Ribonucleic Acid to Yeast Ribosomes

A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit

Modes of action of erythromycin and thiostrepton as inhibitors of protein synthesis

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