The Study on The Solution Structure of Full Length Primase From Bacillus subtilis

doi:10.16476/j.pibb.2019.0147

CORC > 成都生物研究所 > 中国科学院成都生物研究所 > 食品安全与环境治理领域 > 应用与环境微生物研究

	The Study on The Solution Structure of Full Length Primase From Bacillus subtilis
	Luo Hao 1,2,3; Liu Wen-Lin 1,2,3; Zhou Ying-Qin 1,3; Tao Mei 1,2,3; Liu Zhong-Chuan 1,3; Wang Gang-Gang 1,3
刊名	PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
	2019
卷号	46 期号:11 页码:1101-1109
关键词	DNA replication primase SAXS flexibility
ISSN号	1000-3282
DOI	10.16476/j.pibb.2019.0147
产权排序	1
文献子类	Article
英文摘要	In bacterial DNA replication, DnaG primase synthesizes RNA primers which are then extended by DNA polymerase. The DnaG primase consists of three domains, N-terminal zinc-binding domain (ZBD), RNA polymerase domain (RPD) and C-terminal helicase binding domain (HBD). In the process of producing primers, the three domains of primase cooperate with each other, and none is dispensable. Although the structures of the primase domains have been reported, so far, the full-length structure of the primase is not known yet. Here, the model of full-length DnaG in Bacillus subtilis (BsuDnaG) was constructed from the data of X-ray small angle scattering (SAXS) analysis. The BsuDnaG is in extended state in solution. On the other hand, the ZBD and HBD domains could exhibit continuous conformational changes relative to the RPD domain. This study suggests the domains rearrangement in DnaG primase may facilitate its function in DNA replication.
学科主题	Biochemistry & Biophysics
URL标识	查看原文
WOS关键词	HELICASE-BINDING DOMAIN ; SMALL-ANGLE SCATTERING ; REPLICATION INITIATION ; DNAG ; STEAROTHERMOPHILUS ; CRYSTAL
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics
语种	英语
CSCD记录号	CSCD:6607298
出版者	CHINESE ACAD SCIENCES, INST BIOPHYSICS
WOS记录号	WOS:000498757400007
内容类型	期刊论文
源URL	[http://210.75.237.14/handle/351003/31044]
专题	环境治理与食品安全领域_应用与环境微生物研究
作者单位	1.Chinese Acad Sci, Chengdu Inst Biol, Key Lab Environm & Appl Microbiol, Chengdu 610041, Sichuan, Peoples R China; 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Key Lab Environm Microbiol Sichuan Prov, Chengdu 610041, Sichuan, Peoples R China;
推荐引用方式 GB/T 7714	Luo Hao,Liu Wen-Lin,Zhou Ying-Qin,et al. The Study on The Solution Structure of Full Length Primase From Bacillus subtilis[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2019,46(11):1101-1109.
APA	Luo Hao,Liu Wen-Lin,Zhou Ying-Qin,Tao Mei,Liu Zhong-Chuan,&Wang Gang-Gang.(2019).The Study on The Solution Structure of Full Length Primase From Bacillus subtilis.PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,46(11),1101-1109.
MLA	Luo Hao,et al."The Study on The Solution Structure of Full Length Primase From Bacillus subtilis".PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS 46.11(2019):1101-1109.