Growth at 5 kPa Causes Differential Expression of a Number of Signals in a Bacillus subtilis Strain Adapted to Enhanced Growth at Low Pressure

Astrobiology ◽  
2021 ◽  
Author(s):  
Samantha M. Waters ◽  
José A. Robles-Martínez ◽  
Wayne L. Nicholson
Keyword(s):  
Bacillus Subtilis ◽  
Differential Expression ◽  
Low Pressure ◽  
Subtilis Strain

scholarly journals Complete Genome Sequence of Bacillus subtilis subsp. subtilis Strain ∆6

2016 ◽  
Vol 4 (4) ◽  
Author(s):  
Daniel R. Reuß ◽  
Andrea Thürmer ◽  
Rolf Daniel ◽  
Wim J. Quax ◽  
Jörg Stülke
Keyword(s):  
Bacillus Subtilis ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Full Genome Sequence ◽  
Subtilis Strain ◽  
Full Genome ◽  
Biotechnological Applications ◽  
A Genome ◽  
Subtilis Subsp

Bacillus subtilis ∆6 is a genome-reduced strain that was cured from six prophages and AT-rich islands. This strain is of great interest for biotechnological applications. Here, we announce the full-genome sequence of this strain. Interestingly, the conjugative element ICE Bs 1 has most likely undergone self-excision in B. subtilis ∆6.

scholarly journals Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50

1979 ◽  
Vol 179 (2) ◽  
pp. 333-339 ◽  
Author(s):  
A Y Strongin ◽  
D I Gorodetsky ◽  
I A Kuznetsova ◽  
V V Yanonis ◽  
Z T Abramov ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Serine Proteinase ◽  
Subtilis Strain ◽  
Bacterial Strains ◽  
Terminal Sequence ◽  
Gramicidin S ◽  
Intracellular Enzymes ◽  
Sepharose 4B ◽  
Homologous Enzyme ◽  
Strict Selection

Intracellular serine proteinase was isolated from sporulating cells of Bacillus subtilis Marburg 168 by gramicidin S-Sepharose 4B affinity chromatography. The enzymological characteristics, the amino acid composition and the 19 residues of the N-terminal sequence of the enzyme are reported. The isolated proteinase was closely related to, but not completely identical with, the intracellular serine proteinase of B. subtilis A-50. The divergence between these two intracellular enzymes was less than that between the corresponding extracellular serine proteinases (subtilisins) of types Carlsberg and BPN′!, produced by these bacterial strains. This may be connected with the more strict selection constraints imposed in intracellular enzymes during evolution.

scholarly journals Synchrotron-based FTIR microspectroscopy of chili resistance induced by Bacillus subtilis strain D604 against anthracnose disease

2017 ◽  
Vol 12 (1) ◽  
pp. 255-263 ◽  
Author(s):  
Kanjana Thumanu ◽  
Darawadee Wongchalee ◽  
Mathukorn Sompong ◽  
Piyaporn Phansak ◽  
Toan Le Thanh ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Subtilis Strain ◽  
Anthracnose Disease ◽  
Ftir Microspectroscopy

scholarly journals kinA mRNA is missing a stop codon in the undomesticated Bacillus subtilis strain ATCC 6051

Microbiology ◽  
2008 ◽  
Vol 154 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Kazuo Kobayashi ◽  
Ritsuko Kuwana ◽  
Hiromu Takamatsu
Keyword(s):  
Bacillus Subtilis ◽  
Stop Codon ◽  
Subtilis Strain ◽  
Strain Atcc

Effect of metal ions on lipopeptide secretion from Bacillus subtilis strain FJAT‐4: negative regulation by Ca 2+

2021 ◽  
Author(s):  
Meichun Chen ◽  
Meixia Zheng ◽  
Yanping Chen ◽  
Rongfeng Xiao ◽  
Xuefang Zheng ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Metal Ions ◽  
Negative Regulation ◽  
Subtilis Strain

scholarly journals Complete Genome Sequence of Bacillus subtilis Strain WB800N, an Extracellular Protease-Deficient Derivative of Strain 168

2018 ◽  
Vol 7 (18) ◽  
Author(s):  
Haeyoung Jeong ◽  
Da-Eun Jeong ◽  
Seung-Hwan Park ◽  
Seong Joo Kim ◽  
Soo-Keun Choi
Keyword(s):  
Bacillus Subtilis ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Genetically Engineered ◽  
Subtilis Strain ◽  
Secretory Proteins ◽  
Extracellular Proteases ◽  
Content Type ◽  
Protease Deficient

Bacillus subtilis WB800N is a genetically engineered variant of B. subtilis 168, such that all extracellular proteases are disrupted, which enables WB800N to be widely used for the expression of secretory proteins. Here, we report the 4.2-Mb complete genome sequence of WB800N and present all of the disrupted gene structure.

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