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RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity. [PDF]
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The Peptidyl Transferase Center: a Window to the Past
Microbiology and Molecular Biology Reviews, 2021In his 2001 article, “Translation: in retrospect and prospect,” the late Carl Woese made a prescient observation that there was a need for the then-current view of translation to be “reformulated to become an all-embracing perspective about which 21st century Biology can develop” (RNA 7:1055–1067, 2001, https://doi.org/10.1017 ...
Madhan R. Tirumalai +3 more
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Peptidyl transferase and beyond
Biochemistry and Cell Biology, 1995The peptidyl transferase center of the Escherichia coli ribosome encompasses a number of 50S-subunit proteins as well as several specific segments of the 23S rRNA. Although our knowledge of the role that both ribosomal proteins and 23S rRNA play in peptide bond formation has steadily increased, the location, organization, and molecular structure of ...
Wower, J +5 more
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Transesterification by Peptidyl Transferase
Nature, 1970Peptidyl transferase, the enzyme which catalyses formation of peptide bonds, can be stimulated by CCA, the 3′-terminus of tRNA, to catalyse also a transesterification reaction involving nucleophilic attack of Met-tRNAfMet by ethanol to yield fMet-ethyl ester.
E, Scolnick +3 more
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Masking of peptidyl transferase activity in polyribosomes
Archives of Biochemistry and Biophysics, 1975Abstract The peptidyl transferase activity of polysomes from Escherichia coli , rabbit reticulocytes and chick embryos, assayed in the fragment reaction, is 3- to 10-fold lower than the corresponding activity of single ribosomes. The polysomal peptidyl transferase activity is restored in full under conditions of in vitro protein synthesis that ...
V R, Leick, R F, Santerre, R, Kaempfer
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Molecular aspects of the ribosomal peptidyl transferase
Biochemical Society Transactions, 2002The proteins in a living cell are synthesized on a large bipartite ribonucleoprotein complex termed the ribosome. The peptidyl transferase, which polymerizes amino acids to yield peptides, is localized on the large subunit. Biochemical investigations over the past 35 years have led to the hypothesis that rRNA has a major role in all ribosomal functions.
Barta, Andrea +4 more
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Peptidyl transferase: A new method for kinetic studies
Biochemical and Biophysical Research Communications, 1972The 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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The presence of peptidyl transferase in wheat embryo ribosomes
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971Abstract 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, 1979Arginine 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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