V. V. Kotusov

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50 S subunits of E. coli ribosomes catalyze the reaction of the 2′(3′)-N-(formyl) methionine ester of adenosine 5′-phosphate and Phe-tRNA resulting in peptide bond synthesis. Cytidine 5′-phosphate stimulates this process on 50 S ribosomal subunits as well as on intact ribosomes. The obtained data show that the areas of the peptidyltransferase donor site(More)
The mechanism of 5'-cytidilic acid stimulation of the reaction between 2'(3')-O-formylmethionine ester of 5'-adenylic acid and phenylalanyl-tRNA catalyzed by E. coli ribosomes has been studied. It has been shown that cytidilic acid binds to the donor site of the peptidyltransferase in the area which is usually occupied by the second nucleotide residue of(More)
It has been shown that 50S subunits of E. coli MRE-600 ribosomes catalyze the reaction of N-(formyl)-methionyl ester of adenosine 5'-phosphate acting as peptide donor, with Phe-tRNA or CACCA-Phe serving as a peptide acceptor. The reaction is stimulated by cytidine 5'phosphate and inhibited by lincomycin, puromycin and chloramphenicol. The obtained results(More)
The reaction of 3'(2')-O-(N-formylmethionyl)-adenosine 5'-phosphate with Phe-tRNA or CACCA-Phe catalysed with E. coli MRE-600 ribosomes and stimulated with cytidine 5'-phosphate was investigated. It was shown that the reaction with Phe-tRNA was stimulated within 2--3 times when the temperature has been raised from 0 to 40 degrees. On the contrary when the(More)
Some model substrates of the peptidyl transferase centre of E. coli MRE-600 ribosomes were synthesised and tested in a cell-free system without a template. In these substances the nucleic bases were linked covalently with the ribose residue or had a limited rotation about the glycosidic bond. 3'(2')-O-(N-formylmethionyl)-8-bromoadenosine 5'-phosphate and(More)
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