Protein synthesis in Bacillus subtilis: differential effect of potassium ions on in vitro peptide chain initiation and elongation.
The preparation and fractionation of a highly active and stable in vitro protein-synthesizing system from Bacillus subtilis is described. Potassium satisfied the requirement for a monovalent ion when the initiation factor-dependent binding of formyl-methionyl-transfer ribonucleic acid and synthesis of formyl-methionyl-puromycin were assayed, whereas it inhibited the reactions for polyphenylalanine synthesis. On the other hand, the ammonium ion satisfied the requirement for all assayed reactions. The in vitro experimental evidence suggested that potassium is an inhibitor of one or a few specific reactions involved in peptide chain elongation in B. subtilis.
D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis*; D002250:Carbon Radioisotopes; D002458:Cell Fractionation; D002474:Cell-Free System; D004926:Escherichia coli; D008715:Methionine / Q000378:metabolism; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects*; D010442:Peptide Chain Initiation, Translational / Q000187:drug effects*; D010445:Peptide Elongation Factors / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism; D011188:Potassium / Q000187:drug effects*; D011691:Puromycin / Q000096:biosynthesis; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D010445:Peptide Elongation Factors; D010448:Peptide Initiation Factors; D010649:Phenylalanine; D011691:Puromycin; D012343:RNA, Transfer; D008715:Methionine; D011188:Potassium