A Bacillus subtilis bglA gene encoding phospho-β-glucosidase is inducible and closely linked to a NADH dehydrogenase-encoding gene

Gene ◽  
1994 ◽  
Vol 140 (1) ◽  
pp. 85-90 ◽  
Author(s):  
Jianke Zhang ◽  
Arthur Aronson
Keyword(s):  
Bacillus Subtilis ◽  
Nadh Dehydrogenase ◽  
Gene Encoding ◽  
Encoding Gene

A gene encoding a tyrosine tRNA synthetase is located near Sacs in Bacillus subtilis

DNA Sequence ◽  
1991 ◽  
Vol 1 (4) ◽  
pp. 251-261 ◽  
Author(s):  
P. Glaser ◽  
F. Kunst ◽  
M. Débarbouillé ◽  
A. Vertès ◽  
A. Danchin ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Trna Synthetase ◽  
Gene Encoding

Abstract 319: Adrenergic Hormones Regulate Cardiac Metabolic Health During Embryogenesis

2012 ◽  
Vol 111 (suppl_1) ◽  
Author(s):  
Candice Baker ◽  
Kingsley Osuala ◽  
Steven Ebert
Keyword(s):  
Metabolic Regulation ◽  
Nadh Dehydrogenase ◽  
Energy Levels ◽  
Adenosine Diphosphate ◽  
Metabolic Health ◽  
Energy Utilization ◽  
Cardiovascular Development ◽  
Gene Encoding ◽  
Energy Deficiency ◽  
A Subunit

The adrenergic hormones, norepinephrine (NE) and epinephrine (EPI), are critically important during embryogenesis and cardiovascular development, yet their specific mechanisms of action remain mysterious. Disruption of the dopamine β-hydroxylase (Dbh) gene results in an inability to produce NE and EPI, which leads to death in utero between embryonic days 10.5 (E10.5) and E15.5 from apparent heart failure. To determine genes differentially expressed by the loss of adrenergic hormones, Affymetrix® GeneChip microarray analysis revealed 23 genes (of the 22,000 analyzed) that are significantly altered 2-fold or greater in E10.5 Dbh -/- hearts. Of these altered genes, 31% (7 of 23) are linked to metabolic regulation. The gene encoding for NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, Ndufb2 , for example, is a subunit of the mitochondrial complex 1, and displayed a 2.1-fold change in Dbh -/- embryonic hearts. This led us to investigate the metabolic health of these Dbh -/- embryos. Initially, we measured adenosine triphosphate (ATP) and adenosine diphosphate (ADP) levels in E9.5, E10.5, and E11.5 embryos from Dbh -/- , Dbh +/- , and Dbh +/+ mice. At E9.5, ATP concentrations were similar in Dbh -/- , Dbh +/- , and Dbh +/+ embryos ( p >0.7, n=6), but began to decline in the Dbh -/- embryos at E10.5 compared to Dbh +/- and Dbh +/+ embryos ( p <0.02, n=5). By E11.5, ATP concentrations were markedly decreased in Dbh -/- embryos, while ADP levels were increased 5-fold relative to Dbh +/+ controls. This resulted in a significant ( p <0.01, n=4) and drastic (nearly 50-fold) difference in ATP/ADP ratio (0.4 ± 0.1) in Dbh -/- compared with Dbh +/+ control embryos (20.7 ± 4.1) at E11.5. Despite this dramatic difference in energy levels, all embryos appeared grossly normal, had similar heart rates, and displayed no significant differences in caspase 3 or 7 cleavage activity. Thus, the energy deficiency observed in Dbh -/- embryos did not appear to be associated with preceding signs of distress or demise. These results suggest that adrenergic hormones play an important role in regulating energy production during a critical phase of early development that roughly coincides with the transition from embryonic to fetal stages when increased energy utilization is needed.

scholarly journals Regulation of the Bacillus subtilis bcrC Bacitracin Resistance Gene by Two Extracytoplasmic Function σ Factors

2002 ◽  
Vol 184 (22) ◽  
pp. 6123-6129 ◽  
Author(s):  
Min Cao ◽  
John D. Helmann
Keyword(s):  
Bacillus Subtilis ◽  
Resistance Gene ◽  
Mutant Strain ◽  
Stress Responses ◽  
Double Mutant ◽  
De Novo ◽  
De Novo Synthesis ◽  
Gene Encoding ◽  
Single Promoter ◽  
Higher Sensitivity

ABSTRACT Bacitracin resistance is normally conferred by either of two major mechanisms, the BcrABC transporter, which pumps out bacitracin, or BacA, an undecaprenol kinase that provides C55-isoprenyl phosphate by de novo synthesis. We demonstrate that the Bacillus subtilis bcrC (ywoA) gene, encoding a putative bacitracin transport permease, is an important bacitracin resistance determinant. A bcrC mutant strain had an eightfold-higher sensitivity to bacitracin. Expression of bcrC initiated from a single promoter site that could be recognized by either of two extracytoplasmic function (ECF) σ factors, σX or σM. Bacitracin induced expression of bcrC, and this induction was dependent on σM but not on σX. Under inducing conditions, expression was primarily dependent on σM. As a consequence, a sigM mutant was fourfold more sensitive to bacitracin, while the sigX mutant was only slightly sensitive. A sigX sigM double mutant was similar to a bcrC mutant in sensitivity. These results support the suggestion that one function of B. subtilis ECF σ factors is to coordinate antibiotic stress responses.

scholarly journals A Novel Gene Encoding Xanthan Lyase of Paenibacillus alginolyticus Strain XL-1

2000 ◽  
Vol 66 (9) ◽  
pp. 3945-3950 ◽  
Author(s):  
Harald J. Ruijssenaars ◽  
Sybe Hartmans ◽  
Jan C. Verdoes
Keyword(s):  
Signal Sequence ◽  
Fold Increase ◽  
Side Chain ◽  
Cloning And Sequencing ◽  
Gene Encoding ◽  
E Coli ◽  
Mature Enzyme ◽  
Locust Bean ◽  
Encoding Gene ◽  
Amino Acid Signal

ABSTRACT Xanthan-modifying enzymes are powerful tools in studying structure-function relationships of this polysaccharide. One of these modifying enzymes is xanthan lyase, which removes the terminal side chain residue of xanthan. In this paper, the cloning and sequencing of the first xanthan lyase-encoding gene is described, i.e., thexalA gene, encoding pyruvated mannose-specific xanthan lyase of Paenibacillus alginolyticus XL-1. ThexalA gene encoded a 100,823-Da protein, including a 36-amino-acid signal sequence. The 96,887-Da mature enzyme could be expressed functionally in Escherichia coli. Like the native enzyme, the recombinant enzyme showed no activity on depyruvated xanthan. Compared to production by P. alginolyticus, a 30-fold increase in volumetric productivity of soluble xanthan lyase was achieved by heterologous production in E. coli. The recombinant xanthan lyase was used to produce modified xanthan, which showed a dramatic loss of the capacity to form gels with locust bean gum.

scholarly journals Quantification and Isolation ofBacillus subtilisSpores using Cell Sorting and automated Gating

2019 ◽  
Author(s):  
Marianna Karava ◽  
Felix Bracharz ◽  
Johannes Kabisch
Keyword(s):  
Bacillus Subtilis ◽  
Cell Sorting ◽  
Fluorescent Dyes ◽  
Model Organism ◽  
Gaussian Mixture ◽  
Spore Formation ◽  
Gene Encoding ◽  
Knock Out ◽  
Optimal Separation ◽  
Genome Modifications

AbstractThe Gram-positive bacteriumBacillus subtilisis able to form endospores which have a variety of biotechnological applications. Due to this ability,B. subtilisis as well a model organism for cellular differentiation processes. Sporulating cultures ofBacillus subtilisform sub-populations which include vegetative cells, spore forming cells and spores. In order to readily and rapidly quantify spore formation we employed flow cytometric and fluorescence activated cell sorting techniques in combination with nucleic acid fluorescent staining in order to investigate the distribution of sporulating cultures on a single cell level. Moreover we tested different fluorescent dyes as well as different conditions in order to develop a method for optimal separation of distinct populations during sporulation. Automated gating procedures using k-means clustering and thresholding by gaussian mixture modeling were employed to avoid subjective gating and allow for the simultaneous measurement of controls. We utilized the presented method for monitoring sporulation over time in strains harboring different genome modifications. We identified the different subpopulations formed during sporulation by employing sorting and microscopy. Finally, we employed the technique to show that a double knock-out mutant of the phosphatase gene encoding Spo0E and of the spore killing factor SkfA results in faster spore formation.

scholarly journals The Bacillus subtilis yqjI Gene Encodes the NADP+-Dependent 6-P-Gluconate Dehydrogenase in the Pentose Phosphate Pathway

2004 ◽  
Vol 186 (14) ◽  
pp. 4528-4534 ◽  
Author(s):  
Nicola Zamboni ◽  
Eliane Fischer ◽  
Dietmar Laudert ◽  
Stéphane Aymerich ◽  
Hans-Peter Hohmann ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Glucose Dehydrogenase ◽  
Reducing Power ◽  
Pentose Phosphate ◽  
Gene Encoding ◽  
Metabolic Intermediates ◽  
The Third ◽  
Key Enzyme ◽  
Sequence Similarities

ABSTRACT Despite the importance of the oxidative pentose phosphate (PP) pathway as a major source of reducing power and metabolic intermediates for biosynthetic processes, almost no direct genetic or biochemical evidence is available for Bacillus subtilis. Using a combination of knockout mutations in known and putative genes of the oxidative PP pathway and 13C-labeling experiments, we demonstrated that yqjI encodes the NADP+-dependent 6-P-gluconate dehydrogenase, as was hypothesized previously from sequence similarities. Moreover, YqjI was the predominant isoenzyme during glucose and gluconate catabolism, and its role in the oxidative PP pathway could not be played by either of two homologues, GntZ and YqeC. This conclusion is in contrast to the generally held view that GntZ is the relevant isoform; hence, we propose a new designation for yqjI, gndA, the monocistronic gene encoding the principal 6-P-gluconate dehydrogenase. Although we demonstrated the NAD+-dependent 6-P-gluconate dehydrogenase activity of GntZ, gntZ mutants exhibited no detectable phenotype on glucose, and GntZ did not contribute to PP pathway fluxes during growth on glucose. Since gntZ mutants grew normally on gluconate, the functional role of GntZ remains obscure, as does the role of the third homologue, YqeC. Knockout of the glucose-6-P dehydrogenase-encoding zwf gene was primarily compensated for by increased glycolytic fluxes, but about 5% of the catabolic flux was rerouted through the gluconate bypass with glucose dehydrogenase as the key enzyme.

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