Biochemical characterization of a thermostable HNH endonuclease from deep-sea thermophilic bacteriophage GVE2
Zhang, LK; Huang, YC; Xu DD(徐丹丹); Gong Y(龚勇); Xu, DD; Yang, LX; Qian, KC; Chang, GZ; Gong, Y; Zhou, XJ; Ma, KS
刊名APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
2016
卷号100期号:18页码:8003-8012
关键词Bacteriophage Thermophile HNH motif Endonuclease DNA cleavage Divalent metal ion
DOI10.1007/s00253-016-7568-7
文章类型期刊论文
英文摘要His-Asn-His (HNH) proteins are a very common family of small nucleic acid-binding proteins that are generally associated with endonuclease activity and are found in all kingdoms of life. Although HNH endonucleases from mesophiles have been widely investigated, the biochemical functions of HNH endonucleases from thermophilic bacteriophages remain unknown. Here, we characterized the biochemical properties of a thermostable HNH endonuclease from deep-sea thermophilic bacteriophage GVE2. The recombinant GVE2 HNH endonuclease exhibited non-specific cleavage activity at high temperature. The optimal temperature of the GVE2 HNH endonuclease for cleaving DNA was 60-65 A degrees C, and the enzyme retained its DNA cleavage activity even after heating at 100 A degrees C for 30 min, suggesting the enzyme is a thermostable endonuclease. The GVE2 HNH endonuclease cleaved DNA over a wide pH spectrum, ranging from 5.5 to 9.0, and the optimal pH for the enzyme activity was 8.0-9.0. Furthermore, the GVE2 HNH endonuclease activity was dependent on a divalent metal ion. While the enzyme is inactive in the presence of Cu2+, the GVE2 HNH endonuclease displayed cleavage activity of varied efficiency with Mn2+, Mg2+, Ca2+, Fe2+, Co2+, Zn2+, and Ni2+. The GVE2 HNH endonuclease activity was inhibited by NaCl. This study provides the basis for determining the role of this endonuclease in life cycle of the bacteriophage GVE2 and suggests the potential application of the enzyme in molecular biology and biotechnology.
类目[WOS]Biotechnology & Applied Microbiology
关键词[WOS]GROUP-II INTRONS ; HOMING ENDONUCLEASE ; CRYSTAL-STRUCTURE ; NUCLEASE DOMAIN ; COLICIN E7 ; ESCHERICHIA-COLI ; DNA-BINDING ; CLEAVAGE ; MOTIF ; PROTEIN
语种英语
WOS记录号WOS:000382008000018
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被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/260257
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
中国科学院高能物理研究所_多学科研究中心
作者单位中国科学院高能物理研究所
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Zhang, LK,Huang, YC,Xu DD,et al. Biochemical characterization of a thermostable HNH endonuclease from deep-sea thermophilic bacteriophage GVE2[J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,2016,100(18):8003-8012.
APA Zhang, LK.,Huang, YC.,徐丹丹.,龚勇.,Xu, DD.,...&Ma, KS.(2016).Biochemical characterization of a thermostable HNH endonuclease from deep-sea thermophilic bacteriophage GVE2.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,100(18),8003-8012.
MLA Zhang, LK,et al."Biochemical characterization of a thermostable HNH endonuclease from deep-sea thermophilic bacteriophage GVE2".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 100.18(2016):8003-8012.
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