scholarly journals Transcription of the Bacillus subtilis sacX and sacY genes, encoding regulators of sucrose metabolism, is both inducible by sucrose and controlled by the DegS-DegU signalling system.

1992 ◽  
Vol 174 (19) ◽  
pp. 6087-6095 ◽  
Author(s):  
A M Crutz ◽  
M Steinmetz
Keyword(s):  
Bacillus Subtilis ◽  
Sucrose Metabolism ◽  
Signalling System ◽  
Genes Encoding

scholarly journals Genome sequence analysis of the beneficial Bacillus subtilis PTA-271 isolated from a Vitis vinifera (cv. Chardonnay) rhizospheric soil: assets for sustainable biocontrol

2021 ◽  
Vol 16 (1) ◽  
Author(s):  
Catarina Leal ◽  
Florence Fontaine ◽  
Aziz Aziz ◽  
Conceiçao Egas ◽  
Christophe Clément ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Vitis Vinifera ◽  
Genome Sequence ◽  
Draft Genome ◽  
Rhizospheric Soil ◽  
Bioactive Substances ◽  
Protein Coding ◽  
Genes Encoding ◽  
Stimulate Plant Growth ◽  
Biocontrol Potential

Abstract Background Bacillus subtilis strains have been widely studied for their numerous benefits in agriculture, including viticulture. Providing several assets, B. subtilis spp. are described as promising plant-protectors against many pathogens and as influencers to adaptations in a changing environment. This study reports the draft genome sequence of the beneficial Bacillus subtilis PTA-271, isolated from the rhizospheric soil of healthy Vitis vinifera cv. Chardonnay at Champagne Region in France, attempting to draw outlines of its full biocontrol capacity. Results The PTA-271 genome has a size of 4,001,755 bp, with 43.78% of G + C content and 3945 protein coding genes. The draft genome of PTA-271 putatively highlights a functional swarming motility system hypothesizing a colonizing capacity and a strong interacting capacity, strong survival capacities and a set of genes encoding for bioactive substances. Predicted bioactive compounds are known to: stimulate plant growth or defenses such as hormones and elicitors, influence beneficial microbiota, and counteract pathogen aggressiveness such as effectors and many kinds of detoxifying enzymes. Conclusions Plurality of the putatively encoded biomolecules by Bacillus subtilis PTA-271 genome suggests environmentally robust biocontrol potential of PTA-271, protecting plants against a broad spectrum of pathogens.

scholarly journals Responses of Bacillus subtilis to Hypotonic Challenges: Physiological Contributions of Mechanosensitive Channels to Cellular Survival

2008 ◽  
Vol 74 (8) ◽  
pp. 2454-2460 ◽  
Author(s):  
Tamara Hoffmann ◽  
Clara Boiangiu ◽  
Susanne Moses ◽  
Erhard Bremer
Keyword(s):  
Bacillus Subtilis ◽  
Mutational Analysis ◽  
Mechanosensitive Channels ◽  
High Osmolarity ◽  
Cellular Survival ◽  
Genes Encoding ◽  
Quadruple Mutant ◽  
Rapid Transition ◽  
A Minor ◽  
Small Conductance

ABSTRACT Mechanosensitive channels are thought to function as safety valves for the release of cytoplasmic solutes from cells that have to manage a rapid transition from high- to low-osmolarity environments. Subsequent to an osmotic down-shock of cells grown at high osmolarity, Bacillus subtilis rapidly releases the previously accumulated compatible solute glycine betaine in accordance with the degree of the osmotic downshift. Database searches suggest that B. subtilis possesses one copy of a gene for a mechanosensitive channel of large conductance (mscL) and three copies of genes encoding proteins that putatively form mechanosensitive channels of small conductance (yhdY, yfkC, and ykuT). Detailed mutational analysis of all potential channel-forming genes revealed that a quadruple mutant (mscL yhdY yfkC ykuT) has no growth disadvantage in high-osmolarity media in comparison to the wild type. Osmotic down-shock experiments demonstrated that the MscL channel is the principal solute release system of B. subtilis, and strains with a gene disruption in mscL exhibited a severe survival defect upon an osmotic down-shock. We also detected a minor contribution of the SigB-controlled putative MscS-type channel-forming protein YkuT to cellular survival in an mscL mutant. Taken together, our data revealed that mechanosensitive channels of both the MscL and MscS types play pivotal roles in managing the transition of B. subtilis from hyper- to hypo-osmotic environments.

scholarly journals Identification of the Two Missing Bacterial Genes Involved in Thiamine Salvage: Thiamine Pyrophosphokinase and Thiamine Kinase

2004 ◽  
Vol 186 (11) ◽  
pp. 3660-3662 ◽  
Author(s):  
Jonathan Melnick ◽  
Ewa Lis ◽  
Joo-Heon Park ◽  
Cynthia Kinsland ◽  
Hirotada Mori ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Genes Encoding ◽  
Bacterial Genes

ABSTRACT The genes encoding thiamine kinase in Escherichia coli (ycfN) and thiamine pyrophosphokinase in Bacillus subtilis (yloS) have been identified. This study completes the identification of the thiamine salvage enzymes in bacteria.

scholarly journals The Purine Efflux Pump PbuE in Bacillus subtilis Modulates Expression of the PurR and G-Box (XptR) Regulons by Adjusting the Purine Base Pool Size

2005 ◽  
Vol 187 (2) ◽  
pp. 791-794 ◽  
Author(s):  
Per Nygaard ◽  
Hans H. Saxild
Keyword(s):  
Bacillus Subtilis ◽  
De Novo ◽  
Efflux Pump ◽  
Purine Base ◽  
Purine Bases ◽  
Purine Analogs ◽  
Expression Of Genes ◽  
Genes Encoding ◽  
Transcriptional Fusions

ABSTRACT In Bacillus subtilis, the expression of genes encoding enzymes and other proteins involved in purine de novo synthesis and salvage is affected by purine bases and phosphoribosylpyrophosphate (PRPP). The transcription of the genes belonging to the PurR regulon is negatively regulated by the PurR protein and PRPP. The expression of the genes belonging to the G-box (XptR) regulon, including the pbuE gene, is negatively regulated by a riboswitch-controlled transcription termination mechanism. The G-box regulon effector molecules are hypoxanthine and guanine. pbuE encodes a purine base efflux pump and is now recognized as belonging to a third purine regulon. The expression of the pbuE gene is positively regulated by a riboswitch that recognizes adenine. Here we show that the expression of pbuE′-lacZ transcriptional fusions are induced by adenine to the highest extent in mutants which do not express a functional PbuE pump. In a mutant defective in the metabolism of adenine, the ade apt mutant, we found a high intracellular level of adenine and constitutive high levels of PbuE. A growth test using a purine auxotroph provided further evidence for the role of PbuE in lowering the intracellular concentration of purine bases, including adenine. Purine analogs also affect the expression of pbuE, which might be of importance for the protection against toxic analogs. In a mutant that overexpresses PbuE, the expression of genes belonging to the PurR regulon was increased. Our findings provide further evidence for important functions of the PbuE protein, such as acting as a pump that lowers the purine base pool and affects the expression of the G-box and PurR regulons, including pbuE itself, and as a pump involved in protection against toxic purine base analogs.

scholarly journals Complete Genome Sequence of Bacillus subtilis J-5, a Potential Biocontrol Agent

2017 ◽  
Vol 5 (23) ◽  
Author(s):  
Zhenhua Jia ◽  
Weiwei Jin ◽  
Yali Huang ◽  
Shuishan Song
Keyword(s):  
Bacillus Subtilis ◽  
Biocontrol Agent ◽  
Rhizosphere Soil ◽  
Whole Genome ◽  
Antimicrobial Compounds ◽  
Content Type ◽  
Regulatory Systems ◽  
Potential Biocontrol Agent ◽  
Genes Encoding ◽  
Shed Light

ABSTRACT Bacillus subtilis J-5 was isolated from tomato rhizosphere soil and exhibited strong inhibitory activity against Botrytis cinerea. To shed light on the molecular mechanism underlying the biological control on phytopathogens, the whole genome of this strain was sequenced. Genes encoding antimicrobial compounds and the regulatory systems were identified in the genome.

PTS-Mediated Regulation of the Transcription Activator MtlR from Different Species: Surprising Differences despite Strong Sequence Conservation

2015 ◽  
Vol 25 (2-3) ◽  
pp. 94-105 ◽  
Author(s):  
Philippe Joyet ◽  
Meriem Derkaoui ◽  
Houda Bouraoui ◽  
Josef Deutscher
Keyword(s):  
Bacillus Subtilis ◽  
Lactobacillus Casei ◽  
Sequence Conservation ◽  
Geobacillus Stearothermophilus ◽  
Transcription Activator ◽  
Phosphotransferase System ◽  
Transcription Regulator ◽  
Regulatory Domains ◽  
Genes Encoding ◽  
Enzyme I

The hexitol <smlcap>D</smlcap>-mannitol is transported by many bacteria via a phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS). In most Firmicutes, the transcription activator MtlR controls the expression of the genes encoding the <smlcap>D</smlcap>-mannitol-specific PTS components and <smlcap>D</smlcap>-mannitol-1-P dehydrogenase. MtlR contains an N-terminal helix-turn-helix motif followed by an Mga-like domain, two PTS regulation domains (PRDs), an EIIB<sup>Gat</sup>- and an EIIA<sup>Mtl</sup>-like domain. The four regulatory domains are the target of phosphorylation by PTS components. Despite strong sequence conservation, the mechanisms controlling the activity of MtlR from <i>Lactobacillus casei</i>, <i>Bacillus subtilis</i> and <i>Geobacillus stearothermophilus</i> are quite different. Owing to the presence of a tyrosine in place of the second conserved histidine (His) in PRD2, <i>L. casei</i> MtlR is not phosphorylated by Enzyme I (EI) and HPr. When the corresponding His in PRD2 of MtlR from <i>B. subtilis</i> and <i>G. stearothermophilus</i> was replaced with alanine, the transcription regulator was no longer phosphorylated and remained inactive. Surprisingly, <i>L. casei</i> MtlR functions without phosphorylation in PRD2 because in a <i>ptsI</i> (EI) mutant MtlR is constitutively active. EI inactivation prevents not only phosphorylation of HPr, but also of the PTS<sup>Mtl</sup> components, which inactivate MtlR by phosphorylating its EIIB<sup>Gat</sup>- or EIIA<sup>Mtl</sup>-like domain. This explains the constitutive phenotype of the <i>ptsI</i> mutant. The absence of EIIB<sup>Mtl</sup>-mediated phosphorylation leads to induction of the <i>L. casei</i><i>mtl </i>operon. This mechanism resembles <i>mtlARFD</i> induction in <i>G. stearothermophilus</i>, but differs from EIIA<sup>Mtl</sup>-mediated induction in <i>B. subtilis</i>. In contrast to <i>B. subtilis</i> MtlR, <i>L. casei</i> MtlR activation does not require sequestration to the membrane via the unphosphorylated EIIB<sup>Mtl</sup> domain.

scholarly journals Characterization of Two Kinases Involved in Thiamine Pyrophosphate and Pyridoxal Phosphate Biosynthesis in Bacillus subtilis: 4-Amino-5-Hydroxymethyl-2-Methylpyrimidine Kinase and Pyridoxal Kinase

2004 ◽  
Vol 186 (5) ◽  
pp. 1571-1573 ◽  
Author(s):  
Joo-Heon Park ◽  
Kristin Burns ◽  
Cynthia Kinsland ◽  
Tadhg P. Begley
Keyword(s):  
Bacillus Subtilis ◽  
Pyridoxal Phosphate ◽  
Kinase Activity ◽  
Thiamine Pyrophosphate ◽  
Pyridoxal Kinase ◽  
Genes Encoding

ABSTRACT Two Bacillus subtilis genes encoding two proteins (currently annotated ThiD and YjbV) were overexpressed and characterized. YjbV has 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase activity and should be reannotated ThiD, and B. subtilis ThiD has pyridoxine, pyridoxal, and pyridoxamine kinase activity and should be reannotated PdxK.

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