scholarly journals Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168.

1995 ◽  
Vol 177 (13) ◽  
pp. 3855-3862 ◽  
Author(s):  
T J Smith ◽  
S J Foster
Keyword(s):  
Bacillus Subtilis ◽  
Mother Cell ◽  
Cell Lysis ◽  
Bacillus Subtilis 168

scholarly journals Characterization of a New Sigma-K-Dependent Peptidoglycan Hydrolase Gene That Plays a Role in Bacillus subtilis Mother Cell Lysis

1999 ◽  
Vol 181 (20) ◽  
pp. 6230-6237 ◽  
Author(s):  
Fajar Aji Nugroho ◽  
Hiroki Yamamoto ◽  
Yasuo Kobayashi ◽  
Junichi Sekiguchi
Keyword(s):  
Bacillus Subtilis ◽  
Mother Cell ◽  
Northern Blot Analysis ◽  
Cell Lysis ◽  
Peptidoglycan Hydrolase ◽  
Double Mutation ◽  
Optimum Ph ◽  
High Level ◽  
Extension Analysis

ABSTRACT Bacillus subtilis produces a 30-kDa peptidoglycan hydrolase, CwlH, during the late sporulation phase. Disruption ofyqeE led to a complete loss of CwlH formation, indicating the identity of yqeE with cwlH. Northern blot analysis of cwlH revealed a 0.8-kb transcript after 6 to 7.5 h for the wild-type strain but not for the ςF, ςE, ςG, and ςK mutants. Expression of the ςK-dependent cwlH gene depended on gerE. Primer extension analysis also suggested that cwlH is transcribed by EςK RNA polymerase. CwlH produced in Escherichia coli harboring acwlH plasmid is anN-acetylmuramoyl-l-alanine amidase (EC3.5.1.28 ) and exhibited an optimum pH of 7.0 and high-level binding to the B. subtilis cell wall. A cwlC cwlH double mutation led to a lack of mother cell lysis even after 7 days of incubation in DSM medium, but the single mutations led to mother cell lysis after 24 h.

In vitro characterization of N-terminal truncated EpsC from Bacillus subtilis 168, a UDP-N-acetylglucosamine 4,6-dehydratase

2018 ◽  
Vol 657 ◽  
pp. 78-88 ◽  
Author(s):  
Chinmayi R. Kaundinya ◽  
Handanahal S. Savithri ◽  
K. Krishnamurthy Rao ◽  
Petety V. Balaji
Keyword(s):  
Bacillus Subtilis ◽  
Bacillus Subtilis 168 ◽  
In Vitro Characterization

scholarly journals Biochemical and structural characterization of a β-1,3–1,4-glucanase from Bacillus subtilis 168

2011 ◽  
Vol 46 (5) ◽  
pp. 1202-1206 ◽  
Author(s):  
Gilvan Pessoa Furtado ◽  
Lucas Ferreira Ribeiro ◽  
Camila Ramos Santos ◽  
Celisa Caldana Tonoli ◽  
Angelica Rodrigues de Souza ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Structural Characterization ◽  
Bacillus Subtilis 168

Heterologous expression and characterization of a new heme-catalase in Bacillus subtilis 168

2016 ◽  
Vol 43 (6) ◽  
pp. 729-740 ◽  
Author(s):  
Tuyishime Philibert ◽  
Zhiming Rao ◽  
Taowei Yang ◽  
Junping Zhou ◽  
Genshu Huang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Heterologous Expression ◽  
Bacillus Subtilis 168

scholarly journals Cytochemical studies on alkaline phosphatase production during sporulation in Bacillus subtilis

1975 ◽  
Vol 152 (1) ◽  
pp. 85-89 ◽  
Author(s):  
A R Glenn ◽  
J G Coote
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Subtilis ◽  
Phosphatase Activity ◽  
Strong Correlation ◽  
Mother Cell ◽  
Cytoplasmic Membrane ◽  
Stage Ii ◽  
Biochemical Evidence ◽  
Bacillus Subtilis 168 ◽  
Dense Deposits

During sporulation of Bacillus subtilis 168 there is an increase in activity of alkaline phosphatase in the presence of Pi. This enzyme was shown by cytochemical techniques to be associated with the cytoplasmic membrane of the mother cell and also with the membranes of the developing prespore. There is a strong correlation between an increasing number of electron-dense deposits due to phosphatase activity and the formation of the spore septum, i.e. stage II of sporulation. Cytochemical and biochemical evidence shows that cells well advanced in spore formation can be derepressed to produce the very much higher amounts of alkaline phosphatase characteristic of phosphate-starved vegetative cells.

Characterization of the aminopeptidase from Bacillus subtilis as an extracellular enzyme

1972 ◽  
Vol 18 (12) ◽  
pp. 1883-1891 ◽  
Author(s):  
Fred W. Wagner ◽  
A. Chung ◽  
Lee E. Ray
Keyword(s):  
Bacillus Subtilis ◽  
Regulatory Mechanism ◽  
Extracellular Enzyme ◽  
Cell Lysis ◽  
Nitrogen Utilization ◽  
Extracellular Medium ◽  
Cobalt Ions ◽  
C 50 ◽  
Inhibited Enzyme

A strain of Bacillus subtilis produced an aminopeptidase detectable in the cultural fluid and in cell-free extracts. Both extracellular and intracellular aminopeptidases hydrolyzed L-leucyl-β-naphthylamide substrate after activation with cobalt ions. In the cultural fluid, trace amounts of activity were present as early as 12 h, but the highest activity was attained between 36 and 96 h. The addition of lysozyme to cultures less than 36 h old inhibited the production of the aminopeptidase of the cultural fluid, but was less effective in older cultures. This trend was correlated to the Gram-variability of the organisms in the culture. Chloramphenicol and oxytetracycline also inhibited enzyme production without affecting normal cell lysis. These data were interpreted to imply that the aminopeptidase of the cultural fluid did not result from the release of the intracellular aminopeptidase by cell lysis, but that it was produced by viable, metabolizing cells, most probably Gram-negative. Chromatography of the cultural fluid on CM-Sephadex C-50 showed an aminopeptidase characteristic of the extracellular medium. The possible implication of this enzyme as a regulatory mechanism for nitrogen utilization by Bacillus subtilis is discussed.

scholarly journals Cytological Analysis of the Mother Cell Death Process during Sporulation in Bacillus subtilis

2007 ◽  
Vol 189 (6) ◽  
pp. 2561-2565 ◽  
Author(s):  
Shigeo Hosoya ◽  
Zuolei Lu ◽  
Yousuke Ozaki ◽  
Michio Takeuchi ◽  
Tsutomu Sato
Keyword(s):  
Bacillus Subtilis ◽  
Mother Cell ◽  
Cell Lysis ◽  
Dna Degradation ◽  
Death Process ◽  
Cytological Analysis ◽  
Membrane Rupture ◽  
Free Spore ◽  
Cell Death Process ◽  
Extracellular Nuclease

ABSTRACT We have identified the following events during the late stage in the mother cell in Bacillus subtilis: spore detachment from the polar site of the mother cell, membrane rupture, cell wall collapse, and release of the free spore. The membrane rupture was followed by mother cell lysis. Moreover, we found that NucB, an extracellular nuclease, is involved in DNA degradation after mother cell lysis.

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