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• W2133809618 abstract "Escherichia coli grew exponentially at a reduced rate in the presence of 50 or 100 μg of trimethoprim/ml if the low-molecular-weight products of folate metabolism or their precursors (thymidine, purines, methionine, glycine, and pantothenate) were supplied in the medium. Folate metabolism was inhibited 99.9% by these concentrations of trimethoprim, but a low level of formylation of methionyl transfer ribonucleic acid (met-tRNA F ) could be detected. However, in a medium containing all major amino acids, nucleosides, and vitamins, formylation of met-tRNA F was undetectable in the presence of trimethoprim. No other amino-masked amino acids were detected, and methionine remained a major amino-terminal amino acid of mature proteins. met-tRNA F was rapidly labeled with exogenous methionine and was associated with 30 s ribosomal subunits and 70 s ribosomes. It was concluded that initiation of protein synthesis can occur with unformylated met-tRNA F in E. coli . Changes in macromolecular composition were associated with the lack of formylation, in particular a fourfold increase in both met-tRNA F and ribosomal subunits. These changes would tend to compensate for the low specific rate of initiation with unformylated met-tRNA F ." @default.
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• W2133809618 date "1973-04-01" @default.
• W2133809618 modified "2023-10-11" @default.
• W2133809618 title "Growth and Initiation of Protein Synthesis in<i>Escherichia coli</i>in the Presence of Trimethoprim" @default.
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• W2133809618 doi "https://doi.org/10.1128/jb.114.1.309-322.1973" @default.
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