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At least 541 records · Page 30Linked to original sources
PubMed1965

Effect of antimicrobial agents on the milky disease bacteria Bacillus popilliae and Bacillus lentimorbus.

The effects of antibiotics, sulfonamides, and other antimicrobial agents on vegetative cultures of five strains of milky disease bacteria were compared with those on Bacillus subtilis Cohn emend. Prazmowski, Staphylococcus aureus Rosenbach, Sarcina lutea Schroeter, Escherichia coli (Migula) Castellani and Chalmers, Saccharomyces pastorianus Hansen, and Mucor ramannianus Moel. Similar numbers of viable cells of each organism were exposed to the test materials by use of an antibiotic-sensitivity disc method adapted from techniques recommended by the Food and Drug Administration in the Federal Register. The results suggest that vancomycin or ristocetin, as well as a few other materials, might be useful in controlling contamination either during culture of the fastidious milky disease bacteria or in large populations of vegetative cells undergoing treatment to induce sporulation. Inhibitory concentrations of vancomycin and ristocetin in shaken-tube tests were much lower than expected in comparison with results of sensitivity-disc tests on the milky disease bacteria. Sublethal concentrations of the two antibiotics elicited some morphological change in the bacteria.

Anti-Bacterial Agents↗
PubMed1966

Production and stabilization of cells of Bacillus popilliae and Bacillus lentimorbus.

Bacillus popilliae and B. lentimorbus grew most rapidly and to the greatest extent in aerated cultures at 30 to 32 C with oxygen absorption rates of 1 mmole of O(2) per min per liter, or above. The control of pH also increased the maximal populations attained. Media were developed which consistently produced cell populations of about 10(9) within 24 to 48 hr in aerated cultures of these two species. The acetic acid produced in highly aerated cultures was shown not to be responsible for the rapid loss of cell viability in stationary phase cultures. However, H(2)O(2) was very lethal to cells of B. popilliae, and this species is known to have the capacity to produce it. Stationary-phase cells were partially stabilized by reducing the availability of oxygen after 24 hr of incubation on a shaker, and the addition of low levels of glucose further stabilized the cells. The most stable cells were those produced in a medium in which 4% Trypticase (BBL) and 0.1% barbituric acid were incorporated. A high percentage of these cells contained refractile bodies visible under a phase microscope. Although these bodies were not heat-resistant and lacked other characteristics of endospores, cells in cultures containing them had reasonably high viability for extended periods, as compared with those in control cultures.

Acetates↗
PubMed1982

Cloning of the Bacillus subtilis sulfanilamide resistance gene in Bacillus subtilis.

A recombinant plasmid was constructed by ligation of chromosomal DNA from a sulfanilamide-resistant strain of Bacillus subtilis to the plasmid vector pUB110 which specifies neomycin resistance. Recombinant molecules generated in vitro were introduced into a B. subtilis recipient strain which carried the recE4 mutation, and selection was for neomycin-sulfanilamide-resistant transformants. A single colony was isolated containing the recombinant plasmid pKO101. This 6.3-megadalton plasmid simultaneously conferred resistance to neomycin and sulfanilamide when transferred into sensitive Rec+ or Rec- cells by either transduction or transformation.

Bacillus subtilis↗
PubMed1983

Molecular cloning with bifunctional plasmid vectors in Bacillus subtilis: isolation of a spontaneous mutant of Bacillus subtilis with enhanced transformability for Escherichia coli-propagated chimeric plasmid DNA.

Hybrid plasmid DNA cloned in Escherichia coli undergoes deletions when returned to competent Bacillus subtilis, even in defined restriction and modification mutants of strain 168. We have isolated a mutant of B. subtilis MI112 which is stably transformed at high frequency by chimeric plasmid DNA propagated in E. coli.

Bacillus subtilis↗
PubMed1985

Translational coupling in Bacillus subtilis of a heterologous Bacillus subtilis-Escherichia coli gene fusion.

Translational coupling was demonstrated in a gene fusion in which the promoter and the N-terminal region of the Bacillus subtilis subtilisin (aprA) gene were fused to a promoterless Tn9-derived chloramphenicol acetyltransferase (CAT; EC 2.3.1.28) gene. Expression of this gene fusion results in the production of a native-sized CAT product, whereas the Tn9-derived CAT gene is usually not translated from its own ribosome binding site in B. subtilis (D. S. Goldfarb, R. L. Rodriguez, and R. H. Doi, Proc. Natl. Acad. Sci. USA 79:5886-5890, 1982). A 178-base-pair deletion, which removed part of the signal peptide and the propeptide of the aprA gene and created a translational stop codon 230 base pairs upstream of the CAT gene ribosome binding site, reduced expression of the CAT gene. A BamHI 10-mer linker insertion into this deletion site, which restored the reading frame and simultaneously removed the translation stop codon, restored CAT gene expression. The data indicate that expression of the CAT gene was dependent on translation of the truncated aprA gene into the ribosome binding site of the CAT gene.

Acetyltransferases↗
PubMed1986

Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis.

The genes encoding the thermostable alpha-amylases of Bacillus stearothermophilus and B. licheniformis were cloned in Escherichia coli, and their DNA sequences were determined. The coding and deduced polypeptide sequences are 59 and 62% homologous to each other, respectively. The B. stearothermophilus protein differs most significantly from that of B. licheniformis in that it possesses a 32-residue COOH-terminal tail. Transformation of E. coli with vectors containing either gene resulted in the synthesis and secretion of active enzymes similar to those produced by the parental organisms. A plasmid was constructed in which the promoter and the NH2-terminal two-thirds of the B. stearothermophilus coding sequence was fused out of frame to the entire mature coding sequence of the B. licheniformis gene. Approximately 1 in 5,000 colonies transformed with this plasmid was found to secrete an active amylase. Hybridization analysis of plasmids isolated from these amylase-positive colonies indicated that the parental coding sequences had recombined by homologous recombination. DNA sequence analysis of selected hybrid genes revealed symmetrical, nonrandom distribution of loci at which the crossovers had resolved. Several purified hybrid alpha-amylases were characterized and found to differ with respect to thermostability and specific activity.

Amino Acid Sequence↗
PubMed1986

Electron-paramagnetic-resonance spectroscopy of Bacillus subtilis cytochrome b558 in Escherichia coli membranes and in succinate dehydrogenase complex from Bacillus subtilis membranes.

Cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex was studied by electron-paramagnetic-resonance (EPR) spectroscopy. The cytochrome amplified in Escherichia coli membranes by expression of the cloned cytochrome gene and in the succinate dehydrogenase complex immunoprecipitated from solubilized B. subtilis membranes, respectively, is shown to be low spin with a highly anisotropic (gmax approximately equal to 3.5) EPR signal. The amino acid residues most likely forming fifth and sixth axial ligands to heme in cytochrome b558 are discussed on the basis of the EPR signal and the recently determined gene sequence (K. Magnusson, M. Philips, J.R. Guest, and L. Rutberg, J. Bacteriol. 166:1067-1071, 1986) and in comparison with other b-type cytochromes.

Bacillus subtilis↗
PubMed1987

Cloning and nucleotide sequencing of genes for a second type of small, acid-soluble spore proteins of Bacillus cereus, Bacillus stearothermophilus, and "Thermoactinomyces thalpophilus".

The nucleotide sequences of the single genes coding for the B-type small, acid-soluble spore proteins (SASP) of Bacillus cereus, B. stearothermophilus, and "Thermoactinomyces thalpophilus" were determined, and the amino acid sequences of all B-type SASP were compared. While this type of SASP showed significant sequence conservation around the two spore protease cleavage sites, alignment of these sequences required the introduction of gaps, and even then only 19 of the residues were conserved exactly in all five proteins. However, all five B-type SASP did contain a large (27 to 35-residue), rather well-conserved amino acid sequence repeat, and four of the five proteins had well-conserved regions of 14 to 17 amino acids which appeared three times.

Amino Acid Sequence↗
PubMed1997

Bacillus subtilis RNase III gene: cloning, function of the gene in Escherichia coli, and construction of Bacillus subtilis strains with altered rnc loci.

The rnc gene of Bacillus subtilis, which has 36% amino acid identity with the gene that encodes Escherichia coli RNase III endonuclease, was cloned in E. coli and shown by functional assays to encode B. subtilis RNase III (Bs-RNase III). The cloned B. subtilis rnc gene could complement an E. coli rnc strain that is deficient in rRNA processing, suggesting that Bs-RNase III is involved in rRNA processing in B. subtilis. Attempts to construct a B. subtilis rnc null mutant were unsuccessful, but a strain was constructed in which only a carboxy-terminal truncated version of Bs-RNase III was expressed. The truncated Bs-RNase III showed virtually no activity in vitro but was active in vivo. Analysis of expression of a copy of the rnc gene integrated at the amy locus and transcribed from a p(spac) promoter suggested that expression of the B. subtilis rnc is under regulatory control.

Bacillus subtilis↗
PubMed1969

Cell-free amino acid-incorporating systems from Bacillus licheniformis and Bacillus stearothermophilus 10.

Cell-free amino acid-incorporating systems were prepared from log-phase cells of Bacillus licheniformis and B. stearothermophilus 10. No differences were observed between the two systems with respect to the types and relative amounts of the ribosomes, the time dependence of incorporation, and the optimal magnesium ion concentration (4 mm). The B. licheniformis system showed greater dependence on added transfer ribonucleic acid (tRNA) and was less stimulated by polyuridylic acid (poly U) than the B. stearothermophilus 10 system. Neither system was saturated at a level of 450 mug of poly U per incubation mixture. The S-100 fraction and the isolated tRNA inhibited incorporation in the B. stearothermophilus 10 system at 55 C but not at 37 C. No such inhibition was observed in the B. licheniformis system at either temperature. The tRNA prepared from B. subtilis, B. licheniformis, or B. stearothermophilus 10 could be used interchangeably in the two cell-free systems.

Bacillus↗
PubMed1995

Inactivation of blasticidin S by Bacillus cereus. V. Purification and characterization of blasticidin S-deaminase mediated by a plasmid from blasticidin S resistant Bacillus cereus K55-S1.

Blasticidin S (BS) deaminase (BSR) from a BS-resistant strain, Bacillus cereus K55-S1, was purified to homogeneity. Molecular weights determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and by gel filtration on HPLC are about 15500 and 35000, respectively, indicating the enzyme is a homodimer. The amino acid composition and N-terminal sequence of BSR are the same as those deduced from the nucleotide sequence of the BS-resistant gene, bsr. The optimum temperature and pH for enzyme activity are 60-65 degrees C and near 10.0, respectively. The activity of BSR is inhibited by Cu2+, Hg2+, and p-chloromercuric benzoate (PCMB). Inhibition by PCMB or HgCl2 is reversible by the addition of SH reagents. The enzyme catalyzes the deamination of BS and its derivatives, but not cytosine nucleosides.

Aminohydrolases↗
PubMed1996

Bacillus stearothermophilus cell shape determinant gene, mreC and mreD, and their stimulation of protease production in Bacillus subtilis.

Protease production stimulating genes were isolated from a soybean protein degrading bacterium, Bacillus stearothermophilus HA19. The cloned fragment stimulated production of a 37-kDa protease in B. subtilis. The nucleotide sequence of the genes and their flanking regions were identical to the B. subtilis cell shape determinant genes mreC and mreD [J. Bacteriol., 176, 6729-6742 (1992); J. Bacteriol., 176, 6717-6728 (1992)]. The mreC and mreD genes in B. subtilis stimulate secretion of a neutral protease (37-kDa), and the protease activity in the culture medium reached 2500 U per ml (approximately 10 times higher than the host strain) after 24 h of cultivation in L broth, suggesting the mreCD genes regulate protease expression and the protease is related to the cell shape determination in Bacilli. The protease productions in B. subtilis carrying mreC or mreD deletion plasmids were not elevated, so the 37-kDa protease stimulation requires both mreC and mreD genes. The extracellular protease was purified, and the molecular mass of the enzyme was 37,000 Da by SDS-polyacrylamide gel electrophoresis and gel filtration. The optimum pH and temperature for the enzyme activity were 7.0 and 50 degrees C, respectively, and the enzyme was stable at pH 7-10. The enzyme was inactivated by EDTA, but not by phenylmethyl sulfonyl fluoride and diisopropyl fluorophosphate.

Amino Acid Sequence↗
PubMed2006

Cytolytic toxin Cyt1Aa of Bacillus thuringiensis synergizes the mosquitocidal toxin Mtx1 of Bacillus sphaericus.

Using the shuttle vector pBU4, the mosquitocidal toxin gene mtx1 from Bacillus sphaericus strain SSII-1 was introduced into an acrystalliferous strain of B. thuringiensis both individually and in combination with the accessory protein gene p20 and the cytolytic protein gene cyt1Aa from B. thuringiensis subsp. israelensis. Bioassay results indicated that the recombinants B-pMT4(Mtx1) and B-pMT9(Mtx1), both individually containing mtx1, had moderate toxicities to binary toxin susceptible and binary toxin resistant Culex quinquefasciatus larvae during the vegetative growth stage, but that their toxicities declined rapidly during the sporulation phase. The LC50 values were 2.5 and 4.8 mg/ml respectively, against 3-4 instar susceptible and resistant larvae for the final sporulated cultures of recombinants B-pMT9(Mtx1), and little toxicity was detected for B-pMT4(Mtx1). Meanwhile, the recombinant B-pMPX2(Mtx1+Cyt1Aa) expressing Mtx1, P20 alone, and Cyt1Aa in combination had stable toxicities during both the vegetative phase and the sporulation phase, with a LC50 ranging from 0.45-0.58 mg/ml. Furthermore, expression of Cyt1Aa appeared to enhance the activity of Mtx1 to target mosquito larvae, suggesting a synergism between Cyt1Aa and Mtx1 toxins.

Animals↗
PubMed2000

Interspecific transformation of Bacillus subtilis competent cells by chromosomal DNA in lysates of protoplasts of Bacillus amyloliquefaciens.

Competent cells of Bacillus subtilis were transformed with chromosomal DNA in lysates of protoplasts of B. subtilis or B. amyloliquefaciens. The interspecific transformation frequency of B. subtilis by cysA in a conserved region was 3.1 x 10(4) transformants per microg DNA, 60 times higher than that for conventional transformation using purified DNA. Increased interspecific transformation frequencies of B. subtilis were also observed for arg-1, lys-1, leuB, aroG, thr-5, hisH, or metC markers outside the conserved region (3.1 x 10 approximately 5.2 x 10(2) transformants per microg DNA). An interspecific cotransformation ratio (33-50%) as high as an intraspecific one (46%) using purified DNA was also detected between cysA and rpsL markers, which are separated by 16 kb on the B. subtilis chromosome. Interspecific double transformation of the cysA-arg-1 or cysA-metC marker was observed, which have not been detected for conventional transformation. The involvement of mutS in the interspecific transformation was not significant.

Bacillus subtilis↗
PubMed2002

Molecular cloning of the gene encoding thermostable endo-1,5-alpha-L-arabinase of Bacillus thermodenitrificans TS-3 and its expression in Bacillus subtilis.

The gene that encodes a thermostable endo-arabinase (called ABN-TS) from Bacillus thermodenitrificans TS-3 was cloned, sequenced, and expressed in the mesophilic B. subtilis. The gene contained an open reading frame consists of 939 bp, which encodes 313 amino acids. The deduced amino acid sequence of the enzyme showed 50, 46, and 36% similarity with endo-arabinase from B. subtilis IFO 3134 (PPase-C), Pseudomonas fluorescens (ArbA), and Aspergillus niger (ABNA), respectively. The hydrophobic and acidic amino acids making up ABN-TS outnumbered those in PPase-C. The gene product expressed in B. subtilis, as the host, had substantially the same characteristics, and was stable up to 70 degrees C, and the reaction was optimal around 70 degrees C, as well as native ABN-TS.

Amino Acid Sequence↗
PubMed2005

Fourier transform infrared reflectance microspectroscopy study of Bacillus subtilis engineered without dipicolinic acid: the contribution of calcium dipicolinate to the mid-infrared absorbance of Bacillus subtilis endospores.

Mid-infrared spectra of spores of two strains of Bacillus subtilis, PS832 (wild-type) and FB122 (sleB spoVF), that are isogenic except for the two mutations in FB122 were obtained by Fourier transform infrared (FT-IR) reflectance microspectroscopy. The mutations in FB122 cause the spores of this strain to be devoid of dipicolinic acid (pyridine-2,6-dicarboxylic acid; DPA), a biomarker characteristic of bacterial spores. Analysis of these two strains by difference spectroscopy revealed a spectrum similar to that of calcium dipicolinate (CaDPA), a chelate salt of DPA. This difference spectrum was compared to mid-infrared spectra of both DPA and CaDPA, and was attributed to CaDPA only. This is the first report known to the authors of a genetically engineered organism being used to identify the spectral contribution of a particular cellular component.

Bacillus subtilis↗