The Study on The Solution Structure of Full Length Primase From Bacillus subtilis | |
其他题名 | The Study on The Solution Structure of Full Length Primase From Bacillus subtilis |
Luo Hao1; Liu WenLin1; Zhou YingQin1; Tao Mei1; Liu ZhongChuan1; Wang GangGang1 | |
发表期刊 | PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS |
ISSN | 1000-3282 |
2019 | |
卷号 | 46期号:11页码:1101-1109 |
关键词 | HELICASE-BINDING DOMAIN SMALL-ANGLE SCATTERING REPLICATION INITIATION DNAG STEAROTHERMOPHILUS CRYSTAL DNA replication primase SAXS flexibility |
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. |
中文摘要 | 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 Cterminal 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. |
收录类别 | CSCD |
语种 | 英语 |
CSCD记录号 | CSCD:6607298 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.yic.ac.cn/handle/133337/35042 |
专题 | 中国科学院烟台海岸带研究所 |
作者单位 | 1.中国科学院 2.中国科学院烟台海岸带研究所 3.中国科学院大学 |
推荐引用方式 GB/T 7714 | Luo Hao,Liu WenLin,Zhou YingQin,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 WenLin,Zhou YingQin,Tao Mei,Liu ZhongChuan,&Wang GangGang.(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. |
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