Bacillus subtilis bacteriophage SPbeta: localization of the prophage attachment site, and specialized transduction

Zahler, Stanley A.; Korman, Ruth Z.; Rosenthal, Richard R.; Hemphill, H. Ernest

doi:10.1128/jb.129.1.556-558.1977

Cited by 96 publications

(38 citation statements)

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“…Bacillus subtilis strains, cell growth and spore preparation The B. subtilis strains used in this work (Table 2) are isogenic with strain CU1065 (Zahler et al 1977;Salzberg and Helmann 2008). For vegetative growth, cells grown overnight on Luria-Bertani (LB) medium plates (Bertani 1951) containing appropriate antibiotics were used to inoculate 5 ml of liquid LB medium containing antibiotics.…”

Section: Methodsmentioning

confidence: 99%

Effects of modification of membrane lipid composition onBacillus subtilissporulation and spore properties

Griffiths

Setlow

2009

Journal of Applied Microbiology

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Aims: To determine effects of inner membrane lipid composition on Bacillus subtilis sporulation and spore properties. Methods and Results: The absence of genes encoding lipid biosynthetic enzymes had no effect on B. subtilis sporulation, although the expected lipids were absent from spores’ inner membrane. The rate of spore germination with nutrients was decreased c. 50% with mutants that lacked the major cardiolipin (CL) synthase and another enzyme for synthesis of a major phospholipid. Spores lacking the minor CL synthase or an enzyme essential for glycolipid synthesis exhibited 50–150% increases in rates of dodecylamine germination, while spores lacking enzymes for phosphatidylethanolamine (PE), phosphatidylserine (PS) and lysylphosphatidylglycerol (l‐PG) synthesis exhibited a 30–50% decrease. Spore sensitivity to H2O2 and tert‐butylhydroperoxide was increased 30–60% in the absence of the major CL synthase, but these spores’ sensitivity to NaOCl or Oxone™ was unaffected. Spores of lipid synthesis mutants were less resistant to wet heat, with spores lacking enzymes for PE, PS or l‐PG synthesis exhibiting a two to threefold decrease and spores of other strains exhibiting a four to 10‐fold decrease. The decrease in spore wet heat resistance correlated with an increase in core water content. Conclusions: Changing the lipid composition of the B. subtilis inner membrane did not affect sporulation, although modest effects on spore germination and wet heat and oxidizing agent sensitivity were observed, especially when multiple lipids were absent. The increases in rates of dodecylamine germination were likely due to increased ability of this compound to interact with the spore’s inner membrane in the absence of some CL and glycolipids. The effects on spore wet heat sensitivity are likely indirect, because they were correlated with changes in core water content. Significance and Impact of the Study: The results of this study provide insight into roles of inner membrane lipids in spore properties.

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Section: Methodsmentioning

confidence: 99%

Effects of modification of membrane lipid composition onBacillus subtilissporulation and spore properties

Griffiths

Setlow

2009

Journal of Applied Microbiology

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“…Bacterial strains Bacillus subtilis. The non-lysogenic strain SB1207 (Viret and Alonso, 1987) derived from strain CU1050 (Zahler et al, 1977) was used for growth of B.subtilis phages and plasmids. SB1207 derivatives TB804 (Trautner et al, 1980) and TB808 (Buhk et al, 1984) carrying the BsuR and BsuF restriction/modification systems respectively were used together with strain SB1207 in the identification of phage SPRc and 03Tc derivatives coding for class I, class UH and-in the case of SPRc-class HM mutant Mtases as described previously (Trautner et al, 1980;Noyer-Weidner et al, 1983;Buhk et al, 1984).…”

Section: Methodsmentioning

confidence: 99%

Sequential order of target-recognizing domains in multispecific DNA-methyltransferases.

et al. 1988

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In the multispecific DNA(cytosine‐5)‐methyltransferases (Mtases) of Bacillus subtilis phages SPR and phi 3T the domains responsible for recognition of DNA methylation targets CCA/TGG, CCGG, GGCC (SPR) and GCNGC, GGCC (phi 3T) represent contiguous sequences of approximately 50 amino acids each. These domains are tandemly arranged and do not overlap. They are part of a ‘variable’ segment within the enzymes which is flanked by ‘conserved’ amino acids, which are very similar amongst bacterial monospecific and the multispecific Mtases studied here. These results follow from a mutational analysis of the SPR and phi 3T Mtase genes. They further support our concept of a modular enzyme organization, according to which variability of type II Mtases with respect to target recognition is achieved by a combination of the same enzyme core with a variety of target‐recognizing domains.

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“…Strain SF109 was found to lack the E1 component enzyme of 2-ketoglutarate dehydrogenase, whereas strain IA70 (citL22) lacked the E3 component enzyme as described by Hoch and Coukoulis (12). Strain IA99, which had been previously designated as having a citK or El mutation (30), was found to be deficient in the E2 component instead. Since no mutation in the E2 component has been previously described, we propose that citM be used to designate mutations in the E2 component of 2-ketoglutarate dehydrogenase.…”

Section: Resultsmentioning

confidence: 81%

Synthesis of oxaloacetate in Bacillus subtilis mutants lacking the 2-ketoglutarate dehydrogenase enzymatic complex

Fisher¹,

Magasanik²

1984

J Bacteriol

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Bacillus subtilis mutants deficient in the 2-ketoglutarate dehydrogenase enzymatic complex required aspartate for growth at wild-type rates on carbon sources for which synthesis of the degradative enzymes is sensitive to catabolite repression (e.g., poor carbon sources), but did not require aspartate for growth on carbon sources which exert catabolite repression (e.g., good carbon sources). Measurement of metabolite pools in a mutant lacking the 2-ketoglutarate dehydrogenase active complex showed that the aspartate requirement for growth on poor carbon sources resulted from a deficiency in intracellular oxaloacetate pools even through pyruvate carboxylase was present at levels corresponding to those in wild-type cells. The oxaloacetate deficiency most likely resulted from the inability of the mutant to regenerate oxaloacetate from citrate due to the enzymatic block in the tricarboxylic acid cycle. Mutants in the enzymes of the dicarboxylic acid half of the citric acid cycle similarly required aspartate for wild-type growth in minimal medium. These results suggested that the complete turning of the tricarboxylic acid cycle is involved in the maintainance of oxaloacetate levels in B. subtilis. The ability of the mutants lacking the 2-ketoglutarate dehydrogenase enzymatic complex to grow at wild-type rates on media containing good carbon sources in the absence of exogenous aspartate is not understood. * Corresponding author. was 0.5% glucose, 0.4% maltose, 0.2% arabinose, or 0.3% inositol. TSS plates contained 1.5% agar. Difco sporulation medium and tryptose blood agar plates have been previously described (27).Growth and mutagenesis. Cells were mutagenized by overnight growth in glucose medium containing 0.05% 2-aminopurine nitrate. TSS cultures were prepared by inoculation of overnight TSS cultures at various cell densities from cells in exponential growth on tryptose blood agar plates. The next day an overnight culture in the exponential or early stationary phase of growth was diluted into or pelleted and suspended in TSS medium at a cell density of 108 per ml.Preparations of extracts and enzyme assays. Cells were grown to mid-log phase (150 Klett units), harvested by centrifugation for 10 min at 10,000 rpm in a Sorvall SS-34 rotor, washed with 0.05 M Tris (pH 7.5) containing 100 mM KCI, and stored at -70°C. Thawed cells were suspended in the same buffer, incubated at 37°C with 250 p,g of lysozyme per ml and 50 ,ug of DNase per ml until lysed, the debris was removed by centrifugation, and the supernatant was used for enzyme assays.Isocitrate dehydrogenase, fumarase, aconitase, and malate dehydrogenase were assayed by the methods of Cox and Hanson (4). Citrate synthase was assayed by the method of Fortnagel and Freese (8). 2-Ketoglutarate dehydrogenase was assayed by monitoring the 2-ketoglutarate-dependent change in absorbance at 340 nm of the reaction mixture containing 0.05 M sodium phosphate (pH 7.5) 0.2 mM coenzyme A, 1 mM NAD+, 4 ,uM thiamine pyrophosphate, 0.1 mM dithiothreitol, 2 mM MgCl2, 5 mM 2-ketogluta...

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Bacillus subtilis bacteriophage SPbeta: localization of the prophage attachment site, and specialized transduction

Abstract: The attachment site for the prophage of SP,8 lies between ilvA and kauA on the chromosome of Bacillus subtilis strain 168. Specialized transduction of citK and kauA can be carried out by certain lysates of SPJ3. It has recently been found (F.

Cited by 96 publications

References 4 publications

Effects of modification of membrane lipid composition onBacillus subtilissporulation and spore properties

Effects of modification of membrane lipid composition onBacillus subtilissporulation and spore properties

Sequential order of target-recognizing domains in multispecific DNA-methyltransferases.

Synthesis of oxaloacetate in Bacillus subtilis mutants lacking the 2-ketoglutarate dehydrogenase enzymatic complex

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