Results 211 to 220 of about 33,890 (233)

Specificity of lincomycin action on peptidyl transferase activity

Biochemical and Biophysical Research Communications, 1979
Abstract The antibiotic lincomycin and twelve of its analogs were analyzed for their effects on three peptidyl transferase reactions, peptide bond formation, esterification, and hydrolysis of formylmethionyl-tRNA. Only lincomycin stimulated hydrolysis while having inhibitory effects on the other two reactions. The effects of the analogs were variable.
J M, Campbell, F, Reusser, C T, Caskey
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Differential effects of antibiotics on peptidyl transferase reactions

Biochemical and Biophysical Research Communications, 1972
Abstract Some of peptidyl transferase inhibitors were found to exhibit different effects on the first and second peptide bond formation on the ribosome. Mikamycin B stimulated fMet-puromycin reaction, but inhibited fMet-Ala-puromycin reaction. The accumulation of fMet-Ala was observed in the presence of mikamycin B, while f2 RNA-directed synthesis of
K, Kubota, A, Okuyama, N, Tanaka
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Peptidyl transferase: A new method for kinetic studies

Biochemical and Biophysical Research Communications, 1972
The reaction of N-Acetyl-phenylalanyl-t-RNA with E.coli ribosomes in the presence of poly Uridylic acid, guanosine 5′-triphosphate, and initiation factors (ribosomal wash), leads to the formation of N-Acetyl-phenylalanyl-RNA-ribosome-poly Uridylic acid complex, which can be isolated on a cellulose nitrate filter.
R, Fico, C, Coutsogeorgopoulos
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Peptidyl Transferase Center of Rat-Liver Ribosome Cores

European Journal of Biochemistry, 1977
Protein-deficient particles have been obtained by treating rat liver 80-S ribosomes or their 60-S subunits with 1 M NH4Cl in the presence of 50% ethanol at 0 degrees C (Po-cores) and 37 degrees C (P37-cores). The Po-cores from 80-S ribosomes are totally inactive in polyphenylalanine synthesis but fully active in the 'fragment assay' to test peptidyl ...
R, Reyes, D, Vázquez, J P, Ballesta
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Possible relationship of peptidyl transferase binding sites, 5S RNA and peptidyl-tRNA

Biochemical and Biophysical Research Communications, 1971
Abstract A possible role of the 5S RNA in the peptide chain elongation process is suggested. This role consists of an interaction of the ψ loop of peptidyl tRNA at the P-site of peptidyl transferase with the single stranded region of the 5S RNA.
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tRNA-rRNA interactions and peptidyl transferase.

The FASEB Journal, 1993
The extent to which ribosomal RNA is directly involved in the function of ribosomes has important implications for both the mechanism of translation and the molecular origins of life. Detailed evidence has accumulated that places the anticodon and acceptor ends of tRNA in close proximity to conserved features of rRNA in the ribosome. Recent studies are
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Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures

Science, 1992
Peptidyl transferase, the ribosomal activity responsible for catalysis of peptide bond formation, is resistant to vigorous procedures that are conventionally employed to remove proteins from protein-nucleic acid complexes. When the "fragment reaction" was used as a model assay for peptide bond formation, Escherichia coli
H F, Noller, V, Hoffarth, L, Zimniak
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Peptidyl Transferase of Bacterial Ribosome: Resistance to Proteinase K

European Journal of Biochemistry, 1979
70‐S ribosomes and 50‐S ribosomal subunits from Escherichia coli D10 were treated with proteinase K for increasing periods of time. Peptidyl transferase activity and sparsomycin‐induced binding of (U)C‐A‐C‐C‐A‐[3H]Leu‐Ac were tested in the treated particles, the binding of the substrate being more sensitive to the protease than peptide bond formation ...
C, Bernabeu, P, Conde, D, Vázquez, J P, Ballesta   +3 more
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The presence of peptidyl transferase in wheat embryo ribosomes

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
Abstract Extensively washed wheat embryo ribosomes require a supernatant factor and GTP in order to synthesize the model peptide N-acetylphenylalanylpuromycin from N-acetylphenylalanyl-tRNA and puromycin. The reaction is inhibited by fusidic acid, suggesting a requirement for translocation.
M, Gatica, J E, Allende
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Interaction of Arginine with the Ribosomal Peptidyl Transferase Centre

European Journal of Biochemistry, 1979
Arginine inhibits the formation of acetylleucyl-puromycin from C(U)-A-C-C-A-LeuAc and puromycin ('fragment reaction'), catalized by Escherichia coli and yeast ribosomes. From 18 different L-amino acids assayed, arginine was the most effective in producing inhibition (50% inhibition at 20 mM, with 1 mM puromycin).
E, Palacián, D, Vázquez
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