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Structural and functional characterization of deep-sea thermophilic bacteriophage gve2 hnh endonuclease
Zhang, Likui1,5,6; Xu, Dandan2,3; Huang, Yanchao1; Zhu, Xinyuan1; Rui, Mianwen1; Wan, Ting1; Zheng, Xin4; Shen, Yulong5; Chen, Xiangdong6; Ma, Kesen7
刊名Scientific reports
2017-02-13
卷号7页码:13
ISSN号2045-2322
DOI10.1038/srep42542
通讯作者Zhang, likui(lkzhang@yzu.edu.cn) ; Gong, yong(yonggong@ihep.ac.cn)
英文摘要Hnh endonucleases in bacteriophages play a variety of roles in the phage lifecycle as key components of phage dna packaging machines. the deep-sea thermophilic bacteriophage geobacillus virus e2 (gve2) encodes an hnh endonuclease (gve2 hnhe). here, the crystal structure of gve2 hnhe is reported. this is the first structural study of a thermostable hnh endonuclease from a thermophilic bacteriophage. structural comparison reveals that gve2 hnhe possesses a typical beta beta alpha-metal fold and zn-finger motif similar to those of hnh endonucleases from other bacteriophages, apart from containing an extra a-helix, suggesting conservation of these enzymes among bacteriophages. biochemical analysis suggests that the alanine substitutions of the conserved residues (h93, n109 and h118) in the hnh motif of gve2 hnhe abolished 94%, 60% and 83% of nicking activity, respectively. compared to the wild type enzyme, the h93a mutant displayed almost the same conformation while the n108a and h118a mutants had different conformations. in addition, the wild type enzyme was more thermostable than the mutants. in the presence of mn2+ or zn2+, the wild type enzyme displayed distinct dna nicking patterns. however, high mn2+ concentrations were needed for the n109a and h118a mutants to nick dna while zn2+ inactivated their nicking activity.
WOS关键词RESTRICTION-ENDONUCLEASE ; DNA-BINDING ; CRYSTAL-STRUCTURE ; COLICIN E7 ; NUCLEASE DOMAIN ; CLEAVAGE ; MECHANISM ; COMPLEX ; PROTEIN ; SITE
WOS研究方向Science & Technology - Other Topics
WOS类目Multidisciplinary Sciences
语种英语
出版者NATURE PUBLISHING GROUP
WOS记录号WOS:000393779500001
内容类型期刊论文
URI标识http://www.corc.org.cn/handle/1471x/2176836
专题高能物理研究所
通讯作者Zhang, Likui; Gong, Yong
作者单位1.Yangzhou Univ, Dept Environm Sci & Engn, Marine Sci & Technol Inst, Yangzhou 225009, Jiangsu, Peoples R China
2.Anhui Univ, Inst Hlth Sci, Hefei 230601, Anhui, Peoples R China
3.Anhui Univ, Sch Life Sci, Hefei 230601, Anhui, Peoples R China
4.Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100864, Peoples R China
5.Shandong Univ, State Key Lab Microbial Technol, Jinan, Peoples R China
6.Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Peoples R China
7.Univ Waterloo, Dept Biol, Waterloo, ON N2L 3G1, Canada
推荐引用方式
GB/T 7714
Zhang, Likui,Xu, Dandan,Huang, Yanchao,et al. Structural and functional characterization of deep-sea thermophilic bacteriophage gve2 hnh endonuclease[J]. Scientific reports,2017,7:13.
APA Zhang, Likui.,Xu, Dandan.,Huang, Yanchao.,Zhu, Xinyuan.,Rui, Mianwen.,...&Gong, Yong.(2017).Structural and functional characterization of deep-sea thermophilic bacteriophage gve2 hnh endonuclease.Scientific reports,7,13.
MLA Zhang, Likui,et al."Structural and functional characterization of deep-sea thermophilic bacteriophage gve2 hnh endonuclease".Scientific reports 7(2017):13.
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