Results 191 to 200 of about 6,691 (210)

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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Ribosomal Components of the Peptidyl Transferase Center

1984
The past years have seen tremendous progress in our knowledge of the structures of ribosomal proteins and RNA (for review articles see Wittmann 1983; Noller 1984, Wollenzien et al. 1984). Yet our understanding of the ribosomal mechanisms has remained rather fragmentary.
E. Küchler, G. Steiner, A. Barta
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Isomers of Aminoacyl- and Peptidyl-tRNA in the Peptidyl Transferase Reaction

1986
The synthesis of the peptide bonds takes place via the transfer of the activated peptidyl residue from peptidyl-tRNA to the aminoacyl residue of aa-tRNA. Although the ester bond of charged tRNAs is an energy-rich bond with the free energy of hydrolysis approximately equal to the free energy of hydrolysis of ATP (Loftfield, 1972), the reaction between ...
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Identifying the peptidyl transferase centre

Trends in Biochemical Sciences, 1982
R.A. Garrett, Paul Wooley
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