Results 181 to 190 of about 6,691 (210)

Transesterification by Peptidyl Transferase

Nature, 1970
Peptidyl 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, G, Milman, M, Rosman, T, Caskey   +3 more
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Peptidyl transferase and beyond

Biochemistry and Cell Biology, 1995
The 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, Wower, IK, Kirillov, SV, Rosen, KV, Hixson, SS, Zimmermann, RA   +5 more
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Masking of peptidyl transferase activity in polyribosomes

Archives of Biochemistry and Biophysics, 1975
Abstract 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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Affinity labelling of yeast ribosomal peptidyl transferase

Molecular and General Genetics MGG, 1978
Using p-nitrophenylcarbamyl-phenylalanyl-tRNA (PNPC-Phe-tRNA) and N-Iodoacetylphenylalanyl-tRNA as affinity labels we have attempted to identify the components of the aminoacyl-tRNA binding sites located in the vicinity of the peptidyl transferase centre of the yeast ribosome. Both Phe-tRNA derivatives bind to the ribosomal A-site in the presence of 20
M, Pérez-Gosálbez, D, Vázquez, J P, Ballesta   +2 more
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Molecular aspects of the ribosomal peptidyl transferase

Biochemical Society Transactions, 2002
The 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, Schulmeister, Ulrike, Polacek, Norbert, Panuschka, Claudia, Dorner, Silke   +4 more
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The Peptidyl Transferase Center: a Window to the Past

Microbiology and Molecular Biology Reviews, 2021
In 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, Mario Rivas, Quyen Tran, George E. Fox   +3 more
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SPARK: A New Peptidyl Transferase Activity Assay

2008
The formation of peptide bonds is the central chemical reaction during protein synthesis and is catalyzed by the peptidyl transferase center residing in the large ribosomal subunit. This active site is composed of universally conserved rRNA nucleosides.
Alexander S, Mankin, Norbert, Polacek
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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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