Appl Environ Microbiol
February 1992
A medium consisting of MYPGP agar supplemented with vancomycin was found to be highly selective for Bacillus popilliae, especially for strains originally isolated from Japanese beetle larvae. The medium has proven to be useful for the quantitation of B. popilliae spores in commercial spore powder and in soil.
View Article and Find Full Text PDFMcDonald and Burke (J. Bacteriol. 149:391-394, 1982) previously cloned a sulfanilamide-resistance gene, sul, residing on a 4.
View Article and Find Full Text PDFAppl Environ Microbiol
September 1985
An electron microscopic study of sporulation of Bacillus larvae, a honeybee pathogen, in TMYGP broth (D. W. Dingman and D.
View Article and Find Full Text PDFAppl Environ Microbiol
March 1985
Protoplasts of Bacillus larvae NRRL b-3555 and Bacillus subtilis RM125 (restrictionless, modificationless mutant) were transfected with DNA from the B. larvae bacteriophage PBL1c in the presence of polyethylene glycol. B.
View Article and Find Full Text PDFAppl Environ Microbiol
June 1984
Sporulation of Bacillus larvae NRRL B-3650 occurred only at aeration rates lower than those used for cultivation of most Bacillus species. One possible explanation for the requirement for a low level of aeration in B. larvae is that toxic forms of oxygen such as H(2)O(2) and superoxide are involved.
View Article and Find Full Text PDFTwo temperate bacteriophages have been isolated from Bacillus larvae: PBL1 and PBL0 .5. Strains lysogenic for either of these phages are immune to lysis by the same phage but are sensitive to the other phage.
View Article and Find Full Text PDFAppl Environ Microbiol
October 1983
A new medium, designated TMYGP broth, was developed that allowed the honeybee pathogen Bacillus larvae NRRL B-3650 to produce up to 5 x 10 spores per ml of culture (microscopic count). This species normally sporulates poorly, if at all, in artificial broth media. An aeration rate lower than that normally used to cultivate other Bacillus species was required for sporulation.
View Article and Find Full Text PDFCan J Microbiol
December 1980
Homoserine dehydrogenase in dialyzed cell extracts of Bacillus subtilis 168 was studied, particularly with regard to inhibition, repression, and level of activity as a function of stage of development (growth and sporulation). It was assayed in the "forward direction" using L-aspartic semialdehyde and NADPH as substrates. Of the potentials inhibitors tested, only cysteine and NADP were found to be effective.
View Article and Find Full Text PDFAn electron microscopic analysis of Bacillus subtilis cells revealed that netropsin blocked sporulation ultrastructurally at stages 0-I. These observations are consistent with previous results which indicated that cells were not committed to sporulation in the presence of the drug. Further, the addition of netropsin up to stage III of sporulation prevented the normal sharp increase in dihydrodipicolinate synthase activity which results in dipicolinic acid accumulation of stage IV.
View Article and Find Full Text PDFBiochem Biophys Res Commun
October 1978
Dihydrodipicolinic acid synthase (L-aspartate-beta-semialdehyde hydro-lyase (adding pyruvate and cyclising), EC 4.2.1.
View Article and Find Full Text PDFThe activity of dihydrodipicolinate synthase increased late in sporulation in Bacillus subtilis. Mutants blocked at several stages of sporulation due to having an altered ribonucleic acid polymerase failed to exhibit this increase.
View Article and Find Full Text PDFA four- to sixfold increase in specific activity of dihydrodipicolinic acid synthase was observed during sporulation of Bacillus cereus. The enzyme from cells harvested before and after the increase in specific activity appeared to be very similar as judged by pH optima, heat denaturation kinetics, apparent Michaelis constants, chromatography on diethylaminoethyl-cellulose and Sephadex G-200, and polyacrylamide gel electrophoresis. Studies with various combinations of amino acids and one of the enzyme substrates, pyruvate, failed to give evidence for control of the enzyme by activation, inhibition, repression, induction, or stabilization.
View Article and Find Full Text PDFRed pigments were extracted from Streptoverticillium rubrireticuli strain 100-19, an organism frequently incriminated in pink staining of polyvinyl chloride. These pigments were identified as undecylprodiginine and butylcycloheptylprodiginine.
View Article and Find Full Text PDFAn intracellular, glucose-containing polysaccharide accumulates in Bacillus cereus early in sporulation and is degraded at the time of spore maturation. This pattern of accumulation and degradation occurred when growth was limited by glucose or a component of yeast extract. These data suggest that the polysaccharide may be serving as a carbon and energy storage compound for sporulation.
View Article and Find Full Text PDFThe extent of incorporation of aspartate into dipicolinic acid and into various amino compounds was determined in Bacillus cereus at various times before, during, and near the end of synthesis of dipicolinic acid. The purpose of this study was to gain further information on the in vivo control of the biosynthesis of amino acids derived from aspartate. Control of the lysine biosynthetic pathway was of particular interest with regard to sporulation, owing to the important role of diaminopimelate and dipicolinate in the structure of the spore.
View Article and Find Full Text PDFl-Lysine caused repression of diaminopimelate decarboxylase synthesis in Bacillus cereus when grown in either a minimal defined medium (CDGS medium) or a complex defined medium (a modified lysine assay medium). When cells were grown in either of the two media, variations in the specific activity of the enzyme as a function of time were found to be correlated with the intracellular lysine pool size during growth. From all of the data presented, it seems reasonable to conclude that during growth the synthesis of diaminopimelate decarboxylase is probably regulated by the intracellular lysine pool size.
View Article and Find Full Text PDFSynthesis of diaminopimelate decarboxylase in 7 of 11 different Bacillus species tested was subject to l-lysine repression.
View Article and Find Full Text PDFThe meso-diaminopimelate (DAP) decarboxylase of Bacillus licheniformis, a pyridoxal phosphate-requiring enzyme, was stabilized in vitro by 0.15 m sodium phosphate buffer (pH 7.0) containing 1 mm 2,3-dimercaptopropan-1-ol, 100 mug of pyridoxal phosphate per ml, and 3 mm DAP.
View Article and Find Full Text PDFBiochim Biophys Acta
February 1968