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Domain analysis of the Edwardsiella tarda ferric uptake regulator

文献类型： 外文期刊

作者： Sun, Kun 1 ; Cheng, Shuang 1 ; Wang, Fang 1 ; Sun, Li 1 ;

作者机构： 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China

2.Chinese Acad Sci, Grad Univ, Beijing, Peoples R China

3.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao, Peoples R China

关键词： domain swapping;Edwardsiella tarda;ferric uptake regulator;mutagenesis

期刊名称：JOURNAL OF GENERAL AND APPLIED MICROBIOLOGY （ 影响因子：1.452； 五年影响因子：1.479 ）

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收录情况： SCI

摘要： Recent studies have shown that the ferric uptake regulator (Fur) of Edwardsiella tarda (Fur_(Et)) shares high sequence identity with the Escherichia coli Fur (Fur_(Ec)) at the N-terminal DNA-binding region. In the present study, the functional importance of the C-terminal region of Fur_(Et) was investigated. It was found that Fur_(Et) bearing deletion of the C-terminal 12 residues still possesses most of the repressor activity, whereas Fur_(Et) bearing deletions of the C-terminal 16 and more than 16 residues are severely affected in activity. Domain swapping analyses indicated that the chimeric Fur proteins (Et75Ec73 and Et75Vh74) consisting of the N-terminal 1-75 region of Fur_(Et) fused to the C-terminal 76-148 region of Fur_(Ec) and the C-terminal 76-149 region of the Vibrio harveyi Fur (Furvh), respectively, are fully active. C92 of Fur_(Ec) and C137 of Fur_(Vh), which are functionally essential in Fur_(Ec) and Furvh, respectively, are also essential in Et75Ec73 and Et75Vh74, respectively. Further study identified an artificial Fur protein, EtMF54, which is composed of the N-terminal 49 residues of Fur_(Et) and five artificial residues. Compared to Fur_(Et), EtMF54 possesses partial Fur activity that is iron-dependent. These results (i) indicate that there exist certain functional/structural compatibilities among Fur_(Et), Fur_(Ec), and Fur_(Vh) the C-terminal region; (ii) provide insights to the potential location of the regulatory ion-binding site of Fur_(Et).

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