Crystal structure and biochemical studies of the bifunctional DNA primase-polymerase from phage NrS-1
文献类型：期刊论文
| 作者 | Guo, HJ; Li, MJ; Wang, TL; Wu, H; Zhou, H; Xu, CY; Yu, F; Liu, XP; He, JH |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2019 |
| 卷号 | 510期号:4页码:573—579 |
| 关键词 | ARCHAEO-EUKARYOTIC PRIMASE REPLICATION PLASMID DOMAIN |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2019.01.144 |
| 文献子类 | 期刊论文 |
| 英文摘要 | A novel DNA polymerase found in the deep-sea vent phage NrS-1, was confirmed to have both DNA polymerase and primase activities. In this polymerase, the N-terminal residues 1-300 (referred to as N300) are the core region required for polymerizing DNA and catalyzing de novo DNA synthesis. Here, the crystal structure of N300 was solved at a resolution of 1.80 angstrom. The overall structure consists of a prim/pol domain and a helix bundle domain, which are separated by a 14-residue-long flexible tether (residues 177-190). Both the prim/pol domain of N300 and other primase-polymerases (prim-pol) encompass an analogous fold with conserved catalytic residues. Mutagenesis and enzymatic activity assays show that the acidic active-site residue E139 is required for both polymerase and primase activities. Functional assays confirm the essentiality of the helix bundle domain for primase activity. Furthermore, we identified a mutant (N300-Y261A) of the helix bundle domain, which probably plays an indispensable role in the primer initiation and recognition of template DNA. (C) 2019 Elsevier Inc. All rights reserved. |
| 语种 | 英语 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/31536]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 作者单位 | 1.Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, State Key Lab Microbial Metab, 800 Dongchuan Rd, Shanghai 200240, Peoples R China; 2.Chinese Acad Sci, Shanghai Inst Appl Phys, Shanghai 201800, Peoples R China; 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Guo, HJ,Li, MJ,Wang, TL,et al. Crystal structure and biochemical studies of the bifunctional DNA primase-polymerase from phage NrS-1[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2019,510(4):573—579. |
| APA | Guo, HJ.,Li, MJ.,Wang, TL.,Wu, H.,Zhou, H.,...&He, JH.(2019).Crystal structure and biochemical studies of the bifunctional DNA primase-polymerase from phage NrS-1.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,510(4),573—579. |
| MLA | Guo, HJ,et al."Crystal structure and biochemical studies of the bifunctional DNA primase-polymerase from phage NrS-1".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 510.4(2019):573—579. |
入库方式： OAI收割
来源：上海应用物理研究所
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