Junfeng Li1, NY Hirimuthugoda 2*, Hongfang Li1 and Shumin Yao3
1 Qingdao University of Science & Technology, Zhengzhou Road, No.53, Qingdao, China 266042
2 Department of Animal Science, Faculty of Agriculture, University of Ruhuna, Mapalana, Kamburupitiya, Sri Lanka.
3 Qufu Normal University, Jingxuanxi Road, No.21, Qufu, China 273165
Abstrsact
The complete fur gene from the marine probiotic Alteromonas aurantia A18 was amplified by PCR and the cloned gene was sequenced. Results indicated that the similarity between the sequence of the fur gene from strain A18 and that from Alteromonas sp O-7 was 97%. Fur protein of strain A18 was 98% identical to that of Alteromonas sp. O-7 and 70% identical to that of E. coli.The putative fur open reading frame coded for 148 amino acids representing a protein
of 16.637 kDa. The recombinant expression vector pQE30-fur was constructed to confirm
function of the cloned fur gene in E. coli. We found that siderophore yields of the transformants
bearing pQE30-fur (induced by IPTG) were much lower than those of the parental strain and the
same transformants that were not induced by IPTG in the iron-rich medium. The results suggest
that some enzymes responsible for biosynthesis and secretion of siderophores in E. coli were
repressed by the Fur protein encoded by the fur gene from A. aurantia A18.
Key words: Fur gene, marine probiotic bacteria, siderophore, gene cloning
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