Genomic analysis of Bacillus subtilis lytic bacteriophage ϕNIT1 capable of obstructing natto fermentation carrying genes for the capsule-lytic soluble enzymes poly-γ-glutamate hydrolase and levanase
Autor: | Atsuto Suzuki, Keitarou Kimura, Naoki Abe, Tatsuro Ozaki, Jun Kaneko |
---|---|
Rok vydání: | 2017 |
Předmět: |
Gene Expression Regulation
Viral 0301 basic medicine Glycoside Hydrolases Levanase 030106 microbiology Capsules Bacillus Phages Genome Viral Bacillus subtilis Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Microbiology Bacteriophage 03 medical and health sciences Hydrolase Gene cluster Amino Acid Sequence Molecular Biology biology Organic Chemistry Soy Foods Genomics General Medicine Hydrolase Gene biology.organism_classification Bacillus Phage Polyglutamic Acid Solubility Lytic cycle Fermentation Biotechnology |
Zdroj: | SC10201707050012 |
ISSN: | 1347-6947 0916-8451 |
Popis: | Bacillus subtilis strains including the fermented soybean (natto) starter produce capsular polymers consisting of poly-γ-glutamate and levan. Capsular polymers may protect the cells from phage infection. However, bacteriophage ϕNIT1 carries a γ-PGA hydrolase gene (pghP) that help it to counteract the host cell’s protection strategy. ϕNIT had a linear double stranded DNA genome of 155,631-bp with a terminal redundancy of 5,103-bp, containing a gene encoding an active levan hydrolase. These capsule-lytic enzyme genes were located in the possible foreign gene cluster regions between central core and terminal redundant regions, and were expressed at the late phase of the phage lytic cycle. All tested natto origin Spounavirinae phages carried both genes for capsule degrading enzymes similar to ϕNIT1. A comparative genomic analysis revealed the diversity among ϕNIT1 and Bacillus phages carrying pghP-like and levan-hydrolase genes, and provides novel understanding on the acquisition mechanism of these enzymatic genes. |
Databáze: | OpenAIRE |
Externí odkaz: |