A decrease in S-adenosylmethionine synthetase activity increases the probability of spontaneous sporulation
- 1 October 1982
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 152 (1) , 400-410
- https://doi.org/10.1128/jb.152.1.400-410.1982
Abstract
Starting with a relaxed (relA) strain, mutants with reduced activity of adenosine triphosphate:L-methionine S-adenosyl transferase (EC 2.5.1.6; SAM synthetase) were isolated in Bacillus subtilis. One such mutant (gene symbol metE1) had only 3% of the normal SAM synthetase activity but grew almost as well as the parent strain. Another mutant was isolated (gene symbol spdC1) as being able to sporulate continually at a high frequency; it had 1/2 the normal SAM synthetase activity at 33.degree. C. Both mutants continually and spontaneously entered spore development at a higher frequency than the parent strain in a medium containing excess glucose, ammonium ions and phosphate. Sporulation was prevented by a high concentration of SAM (1 mM or more) or by the combination of adenosine and methionine (0.5 mM or more each), both of which are precursors of SAM. In contrast to this continual increase in the spore titer, addition of decoyinine, an inhibitor of GMP synthetase, rapidly initiated massive sporulation. Various amino acid analogs also induced sporulation in the relA strain, the methionine analogs ethionine and selenomethionine being most effective.This publication has 17 references indexed in Scilit:
- Initiation of Bacillus subtilis sporulation by the stringent response to partial amino acid deprivation.Journal of Biological Chemistry, 1981
- 5-Methylcytosine in Eukaryotic DNAScience, 1981
- DNA Methylation and Gene FunctionScience, 1980
- S-Adenosylmethionine synthetase from Escherichia coli.Journal of Biological Chemistry, 1980
- STRINGENT CONTROL IN E. COLIAnnual Review of Genetics, 1979
- 1,4-Diaminobutane (Putrescine), Spermidine, and SpermineAnnual Review of Biochemistry, 1976
- Kinetic studies of the mechanism of S-adenosylmethionine synthetase from yeastBiochemistry, 1969
- Comparative studies on methionine, selenomethionine, and their ethyl analogues as substrates for methionine adenosyltransferase from rat liverArchives of Biochemistry and Biophysics, 1967
- PRODUCTION OF S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-ETHIONINE BY YEAST1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951