[Fusion expression of a peptide antibiotic-apidaecin gene in Lactococcus lactis].
The ubiquitin fusion of apidaecin was expressed in Lactococcus lactis, using a novel nisin-inducible expression system. After induction, a specific band could be detected in the extracts of the host strain by Tricine-SDS-PAGE and Western blotting. Production of the fusion was up to 7.2% of the total soluble protein of the host strain. While the fusion was cut by ubiquitin specific protease-UBP1, the product had distinct antibacterial activity.
Sun
C
C
Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China.
Chen
X Z
XZ
Huan
L D
LD
Peng
X X
XX
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D023181:Antimicrobial Cationic Peptides / Q000235:genetics*; D015153:Blotting, Western; D013294:Lactococcus lactis / Q000235:genetics*; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*; D014452:Ubiquitins / Q000235:genetics*
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D011993:Recombinant Fusion Proteins; D014452:Ubiquitins; C061361:apidaecin