Experiments Relating to the Biosynthesis of Bacilysin By JOAN ROSCOE
نویسندگان
چکیده
was produced by a strain of Bacillus subtili8 (A 14) in a chemically defined medium containing glucose, ammonium acetate or ammonium chloride, potassium phosphate and other inorganic salts, and ferric citrate. 2. Under the conditions used growth was diphasic. Bacilysin was formed during the second phase of slower growth, and there was little production during the stationary phase. Nevertheless, bacilysin production occurred when protein synthesis was inhibited by chloramphenicol. It thus appears that there is no obligatory coupling of protein synthesis and bacilysin synthesis. 3. When DL-[1-14C]alanine was added to a growing culture of B. subtili8, 140 was incorporated into bacilysin, which contains an N-terminal alanine residue. 4. Under similar conditions virtually no 14C was incorporated into bacilysin from DL-[2-14C]tyrosine, L-[U-14C]tyrosine or [1-14C]acetate, although these compounds were used by the cell for the biosynthesis of other substances. These results indicate that neither tyrosine nor acetate is a precursor of the fragment of bacilysin which yields tyrosine on hydrolysis with hot 6Nhydrochloric acid. 5. The tyrosine-yielding fragment of bacilysin was labelled with 14C from [1,6-ring-14C2]shikimic acid. The biosynthesis of bacilysin thus appears to involve a diversion from the pathway leading to aromatic amino acids at the shikimic acid stage, or a subsequent one.
منابع مشابه
Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-operatively regulate the production of an antibiotic bacilysin in Bacillus subtilis.
We found that a polycistronic operon (ywfBCDEFG) and a monocistronic gene (ywfH) are required for the biosynthesis of bacilysin in Bacillus subtilis. The disruption of these genes by plasmid integration caused loss of the ability to produce bacilysin, accompanied by a lack of bacilysin synthetase activity in the crude extract. We investigated the regulatory mechanism for bacilysin biosynthesis ...
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