Time filter

Source Type

Ding X.,Key Laboratory of South China Sea Fisheries Resources Exploitation and Utilization | Ding X.,CAS South China Sea Fisheries Research Institute | Ding X.,Sun Yat Sen University | Yin B.,CAS South China Sea Institute of Oceanology | And 4 more authors.
Lecture Notes in Electrical Engineering | Year: 2013

A pair of proper primers were designed and synthesized for Polymerase Chain Reaction (PCR) of anti-bacterial gene aiiA which encodes protein aiiA from marine bacterial genome, according to the gene sequences of aiiA. The plasmid pMD18-ZD02aiiA was constructed after PCR testing of aiiA gene. The gene sequence of aiiA was amplified with proper primers (with active locations by enzymes BamHIand EcoRI) from molding board of pMD18-ZD02aiiA and linked into expression vector pET-17b after it was hydrolyzed by enzymes of BamHI and EcoRI. And then plasmids pET-ZD02aiiA was constructed. The results of hydrolyzation of enzymes, PCR amplification and sequencing demonstrated that the target gene fragments were inserted into vector pET-17b correctly, the sequences of gene aiiA and frame of reading codes were right. Thus, it may provide base for the recombinant express and induced express of anti-bacterial gene from marine bacterium. © 2013 Springer-Verlag.


Ding X.,Key Laboratory of South China Sea Fisheries Resources Exploitation and Utilization | Ding X.,CAS South China Sea Fisheries Research Institute | Sun W.-W.,Sun Yat Sen University | Zhang D.-C.,Key Laboratory of South China Sea Fisheries Resources Exploitation and Utilization | And 6 more authors.
Chinese Journal of Ecology | Year: 2013

By using a pair of degenerate primers designed according to the known conserved sequence of aiiA, the gene aiiA encoding the quorum sensing signal degrading enzyme (AiiA) in the genome of marine bacterium ZD02 was amplified by PCR, and the PCR products (ZD02 aiiA) were cloned, sequenced, and analyzed. The ZD02 aiiA was 753 bp (Genbank accession number: KC756214), containing an open reading frame (ORF) which encoded a polypeptide chain AiiA of 250 amino acids residues with a molecular weight of 28.1 kDa and an isoelectric point value of 4.78. A conservative domain (Lactamase-B) (34AA-235AA) in the sequence was identified, and the 3D structure of deduced AiiA protein was further predicted. This study would provide a foundation for the expression of the sequence and its bio-activity analysis.

Loading Key Laboratory of South China Sea Fisheries Resources Exploitation and Utilization collaborators
Loading Key Laboratory of South China Sea Fisheries Resources Exploitation and Utilization collaborators