Asporogenic Bacillus megaterium mutant 27-36 degrades intrinsically short-lived proteins but fails to convert most of other proteins to a short-lived fraction
Language English Country England, Great Britain Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Bacillus megaterium genetics metabolism ultrastructure MeSH
- Bacterial Proteins metabolism MeSH
- Kinetics MeSH
- Mutation MeSH
- Serine Endopeptidases metabolism MeSH
- Spores, Bacterial genetics metabolism MeSH
- Calcium metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Serine Endopeptidases MeSH
- Calcium MeSH
Asporogenic mutant blocked in the 0-II sporulation stage degraded pulse-labelled proteins in the sporulation medium at the same rate as the parental strain for the first two hours. The degraded fraction was mostly composed of intrinsically short-lived proteins which were degraded even after enriching the medium with amino acids and growth resumption. Proteins accessible to degradation because of nutritional shift down formed a lesser proportion of this fraction. The acceleration of protein turnover in the parent strain during the irreversible sporulation phase was not developed in the mutant. A first order kinetic model of protein degradation was used for parameter estimation. Ca(2+)-dependent intracellular serine proteinase was synthesized in an inactive form, which was activated by increasing Ca2+ concentration to 30 mM.
References provided by Crossref.org
