Open AccessTranscription of gene in an acrystalliferous strain of Bacillus thuringiensis XBU001 positively regulated by the metalloprotease camelysin gene at the onset of stationary phase
Author(s) -
Yin Jia,
Ding Xuezhi,
Xia Liqiu,
Yu Ziquan,
Lv Yuan,
Hu Shengbiao,
Huang Shaoya,
Cao Zhenping,
Xiao Xiuqing
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02247.x
Subject(s) - inha , complementation , microbiology and biotechnology , gene , biology , bacillus thuringiensis , plasmid , gene expression , genetics , bacteria , phenotype , medicine , tuberculosis , pathology , isoniazid
The cal Y gene, encoding metalloprotease camelysin in the Bacillus thuringiensis acrystalliferous strain XBU001, was amplified and sequenced. The camelysin from the cal Y sequence was 199 amino acids in size ( c . 22 000 Da). The temperature‐sensitive plasmid pKESX was used to construct a metalloprotease camelysin‐deficient strain of B. thuringiensis . The cal Y gene was replaced by an erythromycin‐resistant gene in KCTF. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and MS analysis showed that the metalloprotease InhA was not expressed after knocking out the gene cal Y. The temperature‐sensitive plasmid pKPC was used to construct a metalloprotease camelysin complementation strain KCTFC. The InhA protein was found in KCTFC. Analysis of the expression of InhA in the wild‐type strain KCTF12, camelysin‐deficient and complementation strains indicated that inh A expression depended on camelysin. Although camelysin did not directly regulate the expression of the InhA through binding to the promoter of the inh A, the results suggest that camelysin can positively regulate the expression of the InhA protein.