Abstract
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.
MeSH Terms
Bacillus subtilis/metabolism
Bacterial Proteins/biosynthesis
Carbon Radioisotopes
Cell Fractionation
Cell-Free System
Escherichia coli
Methionine/metabolism
Peptide Biosynthesis
Peptide Chain Elongation, Translational/drug effects
Peptide Chain Initiation, Translational/drug effects
Peptide Elongation Factors/metabolism
Peptide Initiation Factors/metabolism
Phenylalanine/metabolism
Potassium/drug effects
Puromycin/biosynthesis
RNA, Transfer/metabolism
Ribosomes/metabolism
Chemicals
Bacterial Proteins
Carbon Radioisotopes
Peptide Elongation Factors
Peptide Initiation Factors
Phenylalanine
Puromycin
RNA, Transfer
Methionine
Potassium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sala F
Bazzicalupo M
Parisi B
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19 references, click to expand
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