Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium

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• 作者：Zhongshan Wang (1)
  Guangjun Wang (1)
  Quanju Xiang (1)
  Yizheng Zhang (1)
  Haiyan Wang (1)
  
• 关键词：ATPase ; Cyanide detoxification ; Gene expression ; Phanerochaete chrysosporium ; Rhodanese ; Sulfurtransferase
• 刊名：Biotechnology Letters
• 出版年：2014
• 出版时间：May 2014
• 年：2014
• 卷：36
• 期：5
• 页码：993-999
• 全文大小：909 KB
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• 作者单位：Zhongshan Wang (1)
  Guangjun Wang (1)
  Quanju Xiang (1)
  Yizheng Zhang (1)
  Haiyan Wang (1)
  
  1. Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, Sichuan Key Laboratory of Molecular Biology and Biotechnology, College of Life Sciences, Sichuan University, 29 Wangjiang Road, Chengdu, 610064, Sichuan Province, China
  
• ISSN：1573-6776

文摘

A sulfurtransferase gene (PcSft) with a coding region of 546?bp was cloned from the filamentous white-rot fungus Phanerochaere chrysosporium. The 181-amino acid protein contains a highly conserved “Rhodanese-like-domain and an ATP-binding site, with a molecular weight of 20.68?kDa. Semi-quantitative RT-PCR showed that the selective expression of PcSft was involved in secondary metabolism. The recombinant PcSFT protein was expressed in E. coli BL21 (DE3) and purified by Ni2+-chelating and size-exclusion chromatography. Its ATPase and sulfurtransferase (SFT) activities were indentified and characterized. PcSFT exhibited optimal SFT activity at pH 8 and 30?°C as well as stability at 20?°C and pH 8. The enzyme’s stability under different temperature and pH P. indicates a potential usefulness for the detoxification of cyanide in the environment.