scholarly journals Cloning and expression of a novel protease gene encoding an extracellular neutral protease from Bacillus subtilis.

1991 ◽  
Vol 173 (20) ◽  
pp. 6364-6372 ◽  
Author(s):  
L Tran ◽  
X C Wu ◽  
S L Wong
Keyword(s):  
Bacillus Subtilis ◽  
Cloning And Expression ◽  
Neutral Protease ◽  
Protease Gene ◽  
Gene Encoding

scholarly journals Expression of the Neutral Protease Gene from a Thermophilic Bacillus sp. BT1 Strain in Bacillus subtilis and Its Natural Host: Identification of a Functional Promoter

2000 ◽  
Vol 182 (14) ◽  
pp. 4104-4107 ◽  
Author(s):  
Branislav Večerek ◽  
Gerard Venema
Keyword(s):  
Bacillus Subtilis ◽  
Natural Host ◽  
Neutral Protease ◽  
Protease Gene ◽  
Reading Frame ◽  
Reverse Transcription Pcr ◽  
Gene Open Reading Frame ◽  
Efficient Expression ◽  
Rapid Amplification ◽  
Host Identification

ABSTRACT The expression of the neutral protease gene (npr) from the thermophilic Bacillus sp. BT1 strain was studied in its natural host and in mesophilic Bacillus subtilis. In the thermophilic BT1 strain, the transcription of the protease gene is initiated from its own promoter, just 5′ to the gene. In contrast, in heterologous B. subtilis this thermophilic nprpromoter does not function, and expression of the npr gene results from transcription originating upstream of an adjacent gene, open reading frame X (ORF X). A functional promoter was identified 5′ to ORF X that is required for efficient expression of thenpr gene in Bacillus subtilis as verified by primer extension, reverse transcription-PCR, and 5′ rapid amplification of cDNA ends experiments. These data suggest that transcriptional signals used in thermophilic Bacillus sp. BT1 strain are different from those used in B. subtilis.

scholarly journals Cloning and expression of LTB in Escherichia coli and Bacillus subtilis

2013 ◽  
Vol 16 (1) ◽  
pp. 13-22 ◽  
Author(s):  
Trang Thi Phuong Phan ◽  
Anh Le Tuan Nguyen ◽  
Hoang Duc Nguyen
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Fusion Protein ◽  
Expression System ◽  
Pharmaceutical Products ◽  
Cloning And Expression ◽  
Gene Encoding ◽  
E Coli ◽  
B Subunit ◽  
The Common

LTB is the B subunit of heat labile toxins (LT) in Escherichia coli ETEC. This subunit is non-toxic but has a high immune response. Therefore, LTB is considered a suitable antigen for partial vaccine against the diarrhea caused by E. coli ETEC. The most important component of partial vaccine is antigen protein. Nowadays, with the advancement of recombinant protein technology, these antigens are mainly produced by the common bacterial expression system as E. coli. However, the recombinant proteins produced by E. coli are often miscellaneous with enterotoxins, which should be removed from pharmaceutical products. Thus, the production of antigen proteins in other expression system without endotoxins like Bacillus subtilis is in attention. We conducted the experiments of cloning and expressing LTB using a novel pHT plasmid that allow the protein to be expressed in both of E. coli and B. subtilis. We were successful to generate plasmid pHT326 and express the gene encoding for the fusion protein of LTB and LysSN-6xHis-TEV in B. subtilis and E. coli. The binding of fusion protein on the columns that have affinity with His-tag was confirmed. This result is about to be applied for the development of partial vaccine aganst the diarrhea as well as the development of some diagnostic kits for ETEC in food or medical waste and kits to detect antibodies against LTB in animals.

Cloning and expression of the gene for neutral protease of Bacillus amyloliquefaciens in Bacillus subtilis

1984 ◽  
Vol 1 (5-6) ◽  
pp. 265-277 ◽  
Author(s):  
Masaru Honjo ◽  
Kazuaki Manabe ◽  
Hiroaki Shimada ◽  
Izumi Mita ◽  
Akira Nakayama ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Bacillus Amyloliquefaciens ◽  
Cloning And Expression ◽  
Neutral Protease
Sign in / Sign up

Export Citation Format

Share Document