CHEN Xiang; LUO Heng; DUAN LiXia; XU QingHe; ZHANG Yong; XU HouQiang

doi:10.3967/0895-3988.2011.01.006

doi: 10.3967/0895-3988.2011.01.006

基金项目: the Natural Sciences Foundation of China (NSFC)(30660043)%the National Basic Research Program of China(2010CB534912)%the Doctoral Program of the Ministry of Education of China(200806570003)%the Governor Talents Foundation of Guizhou Province(200822)

Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

Guizhou Key Laboratory of Animal Genetics, Breeding and Reproduction, College of Animal Science,Guizhou University, Guiyang 550025, Guizhou, China;Ministry of Education Key Laboratory of Green Pesticide and Ago-Bioengineering, Guizhou University, Guiyang 550025,Guizhou,China
Guizhou Key Laboratory of Animal Genetics, Breeding and Reproduction, College of Animal Science,Guizhou University, Guiyang 550025, Guizhou, China;The Provincial Key Laboratory for Agricultural Pest Management of Mountainous Region of Guizhou University, Guiyang 550025,Guizhou,China
Guizhou Key Laboratory of Animal Genetics, Breeding and Reproduction, College of Animal Science,Guizhou University, Guiyang 550025, Guizhou, China
Guizhou Key Laboratory of Animal Genetics, Breeding and Reproduction, College of Animal Science,Guizhou University, Guiyang 550025, Guizhou, China;Ministry of Education Key Laboratory of Green Pesticide and Ago-Bioengineering, Guizhou University, Guiyang 550025,Guizhou,China

Funds: the Natural Sciences Foundation of China (NSFC)(30660043)%the National Basic Research Program of China(2010CB534912)%the Doctoral Program of the Ministry of Education of China(200806570003)%the Governor Talents Foundation of Guizhou Province(200822)

摘要: Objective Bloom's syndrome is an autosomal recessive disorder characterized by genomic instability and a predisposition to many cancers. Mutations of the BLM gene (encoding a BLM helicase) may form a structure of the etiology of this disease. As a global pollutant, mercury poses a major threat to human health. The current study was conducted to elucidate the effects of Hg2+ on the structure and activity of BLM642-1290 recombinant helicase, and to further explore the molecular mechanisms of mercury toxicity to the DNA helicase.Methods The effects of Hg2+ on biological activity and structure of BLM642-1290 recombinant helicase were determined by fluorescence polarized, ultraviolet spectroscopic, and free-phosphorus assay technologies, respectively.Results The helicase activity, the DNA-binding activity, and the ATPase activity of BLM642-1290recombinant helicase were inhibited by Hg2+ treatment. The LMCT (ligand-to-metal charge transition)peaks of the helicase were enhanced with the increase of the Hg2+ level. The LMCT peaks of the same concentration of helicase gradually increased over time.Conclusions The biological activity of BLM642-1290 recombinant helicase is inhibited by Hg2+treatment. The conformation of the helicase is significantly altered by Hg2+. There exist two binding sites between Hg2+ and the helicase, which are located in the amino acid residues 1063-1066 and 940-944 of the helicase, respectively.
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Abstract: Objective Bloom's syndrome is an autosomal recessive disorder characterized by genomic instability and a predisposition to many cancers. Mutations of the BLM gene (encoding a BLM helicase) may form a structure of the etiology of this disease. As a global pollutant, mercury poses a major threat to human health. The current study was conducted to elucidate the effects of Hg2+ on the structure and activity of BLM642-1290 recombinant helicase, and to further explore the molecular mechanisms of mercury toxicity to the DNA helicase.Methods The effects of Hg2+ on biological activity and structure of BLM642-1290 recombinant helicase were determined by fluorescence polarized, ultraviolet spectroscopic, and free-phosphorus assay technologies, respectively.Results The helicase activity, the DNA-binding activity, and the ATPase activity of BLM642-1290recombinant helicase were inhibited by Hg2+ treatment. The LMCT (ligand-to-metal charge transition)peaks of the helicase were enhanced with the increase of the Hg2+ level. The LMCT peaks of the same concentration of helicase gradually increased over time.Conclusions The biological activity of BLM642-1290 recombinant helicase is inhibited by Hg2+treatment. The conformation of the helicase is significantly altered by Hg2+. There exist two binding sites between Hg2+ and the helicase, which are located in the amino acid residues 1063-1066 and 940-944 of the helicase, respectively.
- BLM642-1290 recombinant helicase /
- Structure /
- Enzyme activity /
- Mercury

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doi: 10.3967/0895-3988.2011.01.006

Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

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Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

doi: 10.3967/0895-3988.2011.01.006

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Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

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doi: 10.3967/0895-3988.2011.01.006

Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

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Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

doi: 10.3967/0895-3988.2011.01.006

English Abstract

Effects of Mercury on the Structure and Activity of BLM642-1290 Recombinant Helicase

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