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Asporogenic Bacillus megaterium mutant 27‐36 degrades intrinsically short‐lived proteins but fails to convert most of other proteins to a short‐lived fraction
Author(s) -
Chaloupka Jiří,
Kučerová Helena,
Strnadová Marie,
Votruba Jaroslav,
Ludvík Jiří
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201372
Subject(s) - mutant , bacillus megaterium , protein turnover , intracellular , serine , biochemistry , strain (injury) , cytosol , amino acid , spore , biology , chemistry , protein biosynthesis , enzyme , bacteria , microbiology and biotechnology , genetics , gene , anatomy
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. Ca2+‐dependent intracellular serine proteinase was synthesized in an inactive form, which was activated by increasing Ca2+ concentration to 30 mM.