Results 111 to 120 of about 3,838 (150)

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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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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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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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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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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A peptidyl transferase ribozyme capable of combinatorial peptide synthesis

Bioorganic & Medicinal Chemistry, 2004
The formation of peptide bonds is a key step in both the chemical and biological synthesis of peptides. The ribozyme can use a wide range of amino acids as its substrate for the dipeptide synthesis. A library containing 29 peptides whose synthesis was catalyzed by this unique ribozyme was analyzed by mass spectrometry.
Cui, Zhiyong, Sun, Lele, Zhang, Biliang
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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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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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Two classes of inhibitors of peptidyl transferase activity in eukaryotes

Nature, 1974
THE 12,13-epoxytrichothecenes (Fig. 1) form a group of fungal toxins with a tricyclic trichothecene ring system. (For review, see ref. 1). They have been shown to inhibit protein synthesis in a variety of eukaryotic systems2 and in particular they block peptidyl transferase activity as determined by the puromycin-fragment reaction3. More recent studies
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