نتایج جستجو برای: b subtilis

تعداد نتایج: 914119  

2010
Yang M Ming Zhang W Wei Chen Y Lin Gong Y Sheng

BACKGROUND B. subtilis is an important organism in the biotechnological application. The efficient expression system is desirable in production of recombinant gene products in B. subtilis. Recently, we developed a new inducible expression system in B. subtilis, which directed by B. subtilis maltose utilization operon promoter Pglv. The system demonstrated high-level expression for target protei...

Journal: :Journal of bacteriology 1967
N E Welker L L Campbell

Eight strains of highly amylolytic, sporeforming bacilli (hereafter referred to as Bacillus amyloliquefaciens) were compared with respect to their taxonomic relationship to B. subtilis. The physiological-biochemical properties of these two groups of organisms showed that B. amyloliquefaciens differed from B. subtilis by their ability to grow in 10% NaCl, characteristic growth on potato plugs, i...

2012
Hai-Nan Su Zhi-Hua Chen Xiao-Yan Song Xiu-Lan Chen Mei Shi Bai-Cheng Zhou Xian Zhao Yu-Zhong Zhang

Antimicrobial peptides are promising alternative antimicrobial agents compared to conventional antibiotics. Understanding the mode of action is important for their further application. We examined the interaction between trichokonin VI, a peptaibol isolated from Trichoderma pseudokoningii, and Bacillus subtilis, a representative Gram-positive bacterium. Trichokonin VI was effective against B. s...

Journal: :Journal of bacteriology 1992
P Babitzke P Gollnick C Yanofsky

mtrA of Bacillus subtilis was shown to be the structural gene for GTP cyclohydrolase I, an enzyme essential for folic acid biosynthesis. mtrA is the first gene in a bicistronic operon that includes mtrB, a gene involved in transcriptional attenuation control of the trp genes. mtrA of B. subtilis encodes a 20-kDa polypeptide that is 50% identical to rat GTP cyclohydrolase I. Increased GTP cycloh...

Journal: :The Biochemical journal 1992
P Landini M Bandera B P Goldstein F Ripamonti A Soffientini K Islam M Denaro

MDL 62,879 (formerly GE 2270 A) is a novel antibiotic active against Gram-positive bacteria by inhibiting protein synthesis. MDL 62,879 is not active against Gram-negative bacteria, but inhibits cell-free protein synthesis in extracts from Escherichia coli, and shows a high binding affinity for its elongation factor Tu (EF-Tu). We prepared ribosomes and protein-synthesis elongation factors from...

Journal: :iranian journal of biotechnology 2016
kambiz morabbi heravi garshasb rigi maryam rezaei arjomand amin rostami gholamreza ahmadian

background: chitin is an abundant natural polysaccharide found in fungi, algae, and exoskeleton of insects. several bacterial species are capable of utilizing chitin as their carbon source. these bacteria produce chitinases for degradation of chitin into n-acetyl-d-glucosamine. so far, regulation of the chitinase encoding genes has been studied in different bacterial species. among bacillus spe...

2014
S. Ashe U. J. Maji R. Sen S. Mohanty N. K. Maiti

A polymerase chain reaction (PCR) assay was developed for discrimination of Bacillus subtilis from other members of B. subtilis group as well as rapid identification from environmental samples. Primers ENIF and EN1R from endoglucanase gene were used to amplify a1311 bp DNA fragment. The specificity of the primers was tested with seven reference strains and 28 locally isolated strains of endoglu...

Journal: :Journal of bacteriology 1997
W Wang D H Bechhofer

The rnc gene of Bacillus subtilis, which has 36% amino acid identity with the gene that encodes Escherichia coli RNase III endonuclease, was cloned in E. coli and shown by functional assays to encode B. subtilis RNase III (Bs-RNase III). The cloned B. subtilis rnc gene could complement an E. coli rnc strain that is deficient in rRNA processing, suggesting that Bs-RNase III is involved in rRNA p...

Journal: :The Biochemical journal 2000
J P Müller J Ozegowski S Vettermann J Swaving K H Van Wely A J Driessen

CsaA from the Gram-positive bacterium Bacillus subtilis has been identified previously as a suppressor of the growth and protein-export defect of Escherichia coli secA(Ts) mutants. CsaA has chaperone-like activities in vivo and in vitro. To examine the role of CsaA in protein export in B. subtilis, expression of the csaA gene was repressed. While export of most proteins remained unaffected, exp...

Journal: :Microbiology 1996
K Takemaru M Mizuno Y Kobayashi

We have determined the complete nucleotide sequence of the Bacillus subtilis homologues of the Escherichia coli phosphate-specific transport (pst) genes in the framework of the international B. subtilis genome sequencing project. The pst genes in E. coli form an operon arranged in the order pstS, pstC, pstA, pstB and phoU. In the case of B. subtilis, there are also five ORFs presumably forming ...

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