Template-dependent peptide formation on ribosomes catalyzed by pyridine.
We found that poly(U)-dependent polyphenylalanine synthesis on Escherichia coli ribosomes was extremely accelerated in the presence of a high concentration of pyridine. In this reaction, chemical energy sources, such as ATP and GTP, and soluble protein factors are not required, but the template and ribosomes are essential for the progress of the reaction. The reaction was inhibited by the antibiotics which inhibit the usual bacterial translation process on the ribosomes. These observations clearly demonstrate that the pyridine-catalyzed amino acid condensation reaction proceeds on the ribosome.
Nitta
I
I
Department of Industrial Chemistry, Faculty of Engineering, University of Tokyo.
Ueda
T
T
Watanabe
K
K
D001426:Bacterial Proteins / Q000378:metabolism; D002384:Catalysis; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism; D010452:Peptide Biosynthesis; D010455:Peptides / Q000187:drug effects*; D014176:Protein Biosynthesis / Q000187:drug effects*; D011725:Pyridines / Q000494:pharmacology*; D012346:RNA, Transfer, Amino Acyl; D012270:Ribosomes / Q000187:drug effects*; D012995:Solubility; D013698:Templates, Genetic
D001426:Bacterial Proteins; D010455:Peptides; D011725:Pyridines; D012346:RNA, Transfer, Amino Acyl; C012001:polyphenylalanine; C023666:pyridine