IHEP OpenIR  > 多学科研究中心
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
2016
发表期刊APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷号100期号:18页码:8003-8012
文章类型期刊论文
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.
关键词Bacteriophage Thermophile HNH motif Endonuclease DNA cleavage Divalent metal ion
DOI10.1007/s00253-016-7568-7
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类目Biotechnology & Applied Microbiology
WOS记录号WOS:000382008000018
引用统计
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
专题多学科研究中心
作者单位中国科学院高能物理研究所
推荐引用方式
GB/T 7714
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.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
20160613.pdf(2484KB)期刊论文作者接受稿限制开放CC BY-NC-SA请求全文
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Zhang, LK]的文章
[Huang, YC]的文章
[徐丹丹]的文章
百度学术
百度学术中相似的文章
[Zhang, LK]的文章
[Huang, YC]的文章
[徐丹丹]的文章
必应学术
必应学术中相似的文章
[Zhang, LK]的文章
[Huang, YC]的文章
[徐丹丹]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。