Intracellular proteolytic activity during sporulation of Bacillus megaterium

. 1977 ; 22 (1) : 1-11.

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid00402306

Intracellular proteolytic activity increased during incubation of the sporogenic strain of Bacillus megaterium KM in a sporulation medium together with excretion of an extracellular metalloprotease. The exocellular protease activity in a constant volume of the medium reached a 100-fold value with respect to the intracellular activity. Maximal values of the activity of both the extracellular and intracellular enzyme were reached after 3-5 h of incubation. After 7 h 20-50% cells formed refractile spores. The intracellular proteolytic system hydrolyzed denatured proteins in vitro at a rate up to 150 mug mg-1 h-1 and native proteins at a rate up to 70 mug mg-1 h-1. Degradation of proteins in vivo proceeded from the beginning of transfer to the sporulation medium at a constant rate of 40 mug mg-1 h-1 and the inactivation of beta-galactosidase at a rate of 70 mug mg-1 h-1. The intracellular proteolytic activity was inhibited to 65-88% by EDTA, to 23-76% by PMSF. Proteolysis of denatured proteins was inhibited both by EDTA and PMSF more pronouncedly than proteolysis of native proteins; 50-65% of the activity were localized in protoplasts. Another strain of Bacillus megaterium (J) characterized by a high (up to 90%) and synchronous sporulation activity was found to behave in a similar way, but the rate of protein turnover in this strain was almost twice as high. The asporogenic strain of Bacillus megaterium KM synthesized the exocellular protease in the sporulation medium, but its protein turnover was found to decrease substantially after 3-4 h. The intracellular proteolytic system of the sporogenic strain J and the asporogenic strain KM were also inhibited by EDTA and PMSF.

Zobrazit více v PubMed

J Bacteriol. 1971 Jan;105(1):276-83 PubMed

Biochem Biophys Res Commun. 1965 Sep 22;20(6):692-6 PubMed

Folia Microbiol (Praha). 1966;11(2):82-8 PubMed

J Bacteriol. 1967 May;93(5):1527-33 PubMed

Ann Inst Pasteur (Paris). 1969 Nov;117(5):631-6 PubMed

Folia Microbiol (Praha). 1975;20(4):277-88 PubMed

Ann Inst Pasteur (Paris). 1969 Oct;117(4):461-73 PubMed

Folia Microbiol (Praha). 1970;15(4):267-74 PubMed

J Bacteriol. 1975 Feb;121(2):406-10 PubMed

Ann Inst Pasteur (Paris). 1960 Feb;98 :282-90 PubMed

Biochem J. 1959 Mar;71(3):513-8 PubMed

C R Acad Sci Hebd Seances Acad Sci D. 1971 Mar 29;272(13):1806-9 PubMed

J Bacteriol. 1967 Mar;93(3):1031-44 PubMed

J Bacteriol. 1971 Sep;107(3):815-23 PubMed

Biochem Biophys Res Commun. 1972 Oct 17;49(2):328-34 PubMed

Biochem J. 1968 Oct;109(5):793-801 PubMed

J Bacteriol. 1973 May;114(2):612-7 PubMed

J Biol Chem. 1951 Nov;193(1):265-75 PubMed

J Bacteriol. 1971 Jun;106(3):1016-25 PubMed

Proc Natl Acad Sci U S A. 1972 Feb;69(2):422-6 PubMed

Bull Soc Chim Biol (Paris). 1969 Jun 4;51(1):61-8 PubMed

J Bacteriol. 1972 Aug;111(2):557-65 PubMed

Biochem J. 1968 Oct;109(5):811-8 PubMed

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...