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• W1544167706 abstract "Abstract The initiation of protein synthesis by Streptococcus faecalis grown in folate-free culture occurs without N-formylation or N-acylation of methionyl-tRNAfMet. The biochemical and biophysical properties of the tRNAMet from wild type S. faecalis grown under normal cultural conditions in the presence of folate (plus folate) were determined and compared with the properties of the tRNAMet from wild type cells grown in the absence of folate (minus-folate). Two methionine tRNA species, tRNAfMet and tRNAmMet, were isolated from both the plus- and minus-folate cells by chromatography on BD-cellulose. The tRNAfMet from minus-folate cells could be distinguished from the tRNAfMet from plus-folate cells with the BD-cellulose, reversed-phase chromatography (RPC)-3, and RPC-5 chromatographic systems; however, the tRNAmMet species derived from minus- or plus-folate cells were indistinguishable in all of the systems tested. The unformylated methionyl-tRNAfMet from minus-folate S. faecalis binds more efficiently to salt-washed ribosomes in response to initiation factors and poly(A,G,U) than methionyl-tRNAfMet from plus-folate cells. No ribothymidylic acid is detectable in the enzymic nucleotide hydrolysate of purified minus-folate tRNAfMet derived from minus-folate S. faecalis cells, although this minor nucleotide is present in the tRNAfMet derived from plus-folate S. faecalis and Escherichia coli cells. The Tm values of both plus-folate and minus-folate S. faecalis tRNAfMet resemble those of rat liver and yeast tRNAfMet more closely than either E. coli or Clostridium pasteurianum tRNAfMet. The per cent hyperchromicity is about 30% for all six initiator tRNAs tested. The circular dichroism spectra of the plus- and minus-folate tRNAfMet species, as well as the other procaryotic and the eucaryotic tRNAfMet species, were very similar, but not identical. Methionyl-tRNA synthetase of S. faecalis, Escherichia coli, bakers' yeast, and rat liver are all capable of catalyzing the aminoacylation of plus- and minus-folate S. faecalis tRNAfMet to a comparable extent. The procaryotic, but not the eucaryotic, aminoacyl-tRNA synthetases are capable of catalyzing the aminoacylation of S. faecalis tRNAmMet derived from plus- or minus-folate cells. These results establish that the absence of folate in the growth medium of wild type S. faecalis mediates a structural alteration in the tRNAfMet, and suggest that the ability of wild type minus-folate S. faecalis to initiate protein synthesis without formylation of the tRNAfMet is directly related to the structural modification of the initiator tRNA." @default.
• W1544167706 created "2016-06-24" @default.
• W1544167706 creator A5031909976 @default.
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• W1544167706 date "1974-02-01" @default.
• W1544167706 modified "2023-09-28" @default.
• W1544167706 title "Initiation of Protein Synthesis by Folate-sufficient and Folate-deficient Streptococcus faecalis R" @default.
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• W1544167706 doi "https://doi.org/10.1016/s0021-9258(19)42960-8" @default.
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