Restriction and modification in Bacillus subtilis Marburg 168: Target sites and effects on plasmid transformation

1988 ◽  
Vol 211 (1) ◽  
pp. 186-189 ◽  
Author(s):  
S. Bron ◽  
L. Jannière ◽  
S. D. Ehrlich
Keyword(s):  
Bacillus Subtilis ◽  
Plasmid Transformation ◽  
Target Sites

scholarly journals Intramolecular recombination during plasmid transformation of Bacillus subtilis competent cells.

1982 ◽  
Vol 1 (12) ◽  
pp. 1565-1571 ◽  
Author(s):  
B. Michel ◽  
B. Niaudet ◽  
S.D. Ehrlich
Keyword(s):  
Bacillus Subtilis ◽  
Plasmid Transformation ◽  
Competent Cells ◽  
Intramolecular Recombination

scholarly journals RecA Regulation by RecU and DprA During Bacillus subtilis Natural Plasmid Transformation

2018 ◽  
Vol 9 ◽  
Author(s):  
Ester Serrano ◽  
Begoña Carrasco ◽  
Jamie L. Gilmore ◽  
Kunio Takeyasu ◽  
Juan C. Alonso
Keyword(s):  
Bacillus Subtilis ◽  
Plasmid Transformation

scholarly journals Genetic Recombination in Bacillus subtilis 168: Effect of ΔhelD on DNA Repair and Homologous Recombination

2001 ◽  
Vol 183 (19) ◽  
pp. 5772-5777 ◽  
Author(s):  
Begoña Carrasco ◽  
Silvia Fernández ◽  
Marie-Agnes Petit ◽  
Juan C. Alonso
Keyword(s):  
Dna Repair ◽  
Bacillus Subtilis ◽  
Homologous Recombination ◽  
Genetic Recombination ◽  
Methyl Methanesulfonate ◽  
Plasmid Transformation ◽  
Dna Damaging Agents ◽  
Bacillus Subtilis 168 ◽  
Recombination Repair ◽  
Helicase Iv

ABSTRACT The B. subtilis ΔhelD allele rendered cells proficient in transformational recombination and moderately sensitive to methyl methanesulfonate when present in an otherwise Rec+ strain. The ΔhelD allele was introduced into rec-deficient strains representative of the α (recF strain), β (addA addB), γ (recH), ɛ (ΔrecU), and ζ (ΔrecS) epistatic groups. The ΔhelDmutation increased the sensitivity to DNA-damaging agents ofaddAB, ΔrecU, and ΔrecS cells, did not affect the survival ofrecH cells, and decreased the sensitivity ofrecF cells. ΔhelD also partially suppressed the DNA repair phenotype of other mutations classified within the α epistatic group, namely the recL, ΔrecO, and recR mutations. The ΔhelD allele marginally reduced plasmid transformation (three- to sevenfold) of mutations classified within the α, β, and γ epistatic groups. Altogether, these data indicate that the loss of helicase IV might stabilize recombination repair intermediates formed in the absence of recFLOR and renderrecFLOR, addAB, andrecH cells impaired in plasmid transformation.

Plasmid transformation in Bacillus subtilis

1983 ◽  
Vol 192 (1-2) ◽  
pp. 149-154 ◽  
Author(s):  
Antonio Iglesias ◽  
Piotr Ceglowski ◽  
Thomas A. Trautner
Keyword(s):  
Bacillus Subtilis ◽  
Plasmid Transformation

scholarly journals Plasmid transformation in Bacillus subtilis NB22, an antifungal-antibiotic iturin producer

1990 ◽  
Vol 67 (1-2) ◽  
pp. 227-230 ◽  
Author(s):  
Yuko Matsuno ◽  
Hideji Hiraoka ◽  
Takashi Ano ◽  
Makoto Shoda
Keyword(s):  
Bacillus Subtilis ◽  
Antifungal Antibiotic ◽  
Plasmid Transformation

scholarly journals Bacillus subtilis Mutant LicT Antiterminators Exhibiting Enzyme I- and HPr-Independent Antitermination Affect Catabolite Repression of the bglPH Operon

2002 ◽  
Vol 184 (17) ◽  
pp. 4819-4828 ◽  
Author(s):  
Cordula Lindner ◽  
Michael Hecker ◽  
Dominique Le Coq ◽  
Josef Deutscher
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Catabolite Repression ◽  
Carbon Catabolite Repression ◽  
Phosphotransferase System ◽  
Terminal Domain ◽  
Target Sites ◽  
Enzyme I ◽  
In Cells

ABSTRACT The Bacillus subtilis antiterminator LicT regulates the expression of bglPH and bglS, which encode the enzymes for the metabolism of aryl-β-glucosides and the β-glucanase BglS. The N-terminal domain of LicT (first 55 amino acids) prevents the formation of ρ-independent terminators on the respective transcripts by binding to target sites overlapping these terminators. Proteins of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulate the antitermination activity of LicT by phosphorylating histidines in its two PTS regulation domains (PRDs). Phosphorylation at His-100 in PRD-1 requires the PTS proteins enzyme I and HPr and the phosphorylated permease BglP and inactivates LicT. During transport and phosphorylation of aryl-β-glucosides, BglP is dephosphorylated, which renders LicT active and thus leads to bglPH and bglS induction. In contrast, phosphorylation at His-207 and/or His-269 in PRD-2, which requires only enzyme I and HPr, is absolutely necessary for LicT activity and bglPH and bglS expression. We isolated spontaneous licT mutants expressing bglPH even when enzyme I and HPr were absent (as indicated by the designation “Pia” [PTS-independent antitermination]). Introduced in a ptsHI + strain, two classes of licT(Pia) mutations could be distinguished. Mutants synthesizing LicT(Pia) antiterminators altered in PRD-2 still required induction by aryl-β-glucosides, whereas mutations affecting PRD-1 caused constitutive bglPH expression. One of the two carbon catabolite repression (CCR) mechanisms operative for bglPH requires the ρ-independent terminator and is probably prevented when LicT is activated by P∼His-HPr-dependent phosphorylation in PRD-2 (where the prefix “P∼” stands for “phospho”). During CCR, the small amount of P∼His-HPr present in cells growing on repressing PTS sugars probably leads to insufficient phosphorylation at PRD-2 of LicT and therefore to reduced bglPH expression. In agreement with this concept, mutants synthesizing a P∼His-HPr-independent LicT(Pia) had lost LicT-modulated CCR.

Plasmid transformation in Bacillus subtilis

1981 ◽  
Vol 184 (3) ◽  
pp. 400-404 ◽  
Author(s):  
G. Bensi ◽  
A. Iglesias ◽  
U. Canosi ◽  
T. A. Trautner
Keyword(s):  
Bacillus Subtilis ◽  
Plasmid Transformation

scholarly journals Identification of autodigestion target sites in Bacillus subtilis neutral proteinase

1990 ◽  
Vol 272 (1) ◽  
pp. 93-97 ◽  
Author(s):  
B van den Burg ◽  
V G H Eijsink ◽  
B K Stulp ◽  
G Venema
Keyword(s):  
Bacillus Subtilis ◽  
Elevated Temperatures ◽  
Sequence Data ◽  
Three Dimensional ◽  
Hydrophobic Residues ◽  
Neutral Proteinase ◽  
Sds Page ◽  
Target Sites ◽  
Time Specific ◽  
High Degree

Autocatalytic degradation of purified Bacillus subtilis neutral proteinase was examined under various conditions. At elevated temperatures, under non-inhibitory conditions, mature protein was rapidly degraded, but no accumulation of specific breakdown products occurred. However, by incubating purified neutral proteinase on ice during extended periods of time, specific peptides accumulated. These peptides were analysed by SDS/PAGE and Western blotting, and the N-terminal sequences were determined for the four major peptides, which had sizes of 30, 22, 20 and 15 kDa. Sequence data identified five fission sites in the neutral proteinase, three of which were identical with autodigestion target sites in thermolysin, a thermostable neutral proteinase. Comparison of the identified fission sites of the B. subtilis neutral proteinase with the known substrate-specificity of the enzyme indicated that they were in agreement, showing a preference for the generation of fissions at the N-terminal side of large hydrophobic residues, such as leucine, isoleucine and methionine. These results suggest a high degree of similarity in the three-dimensional structures of B. subtilis neutral proteinase and thermolysin.

Sign in / Sign up

Export Citation Format

Share Document