Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria

被引：12

作者：

Zhou, Yingqin ^{[1
,2
,4
]}

Luo, Hao ^{[1
,2
,4
]}

Liu, Zhongchuan ^{[1
,2
]}

Yang, Mu ^{[1
,2
,4
]}

Pang, Xiaoyun ^{[3
]}

Sun, Fei ^{[3
]}

Wang, Ganggang ^{[1
,2
]}

机构：

[1] Chinese Acad Sci, Chengdu Inst Biol, Key Lab Environm & Appl Microbiol, Chengdu 610041, Peoples R China

[2] Key Lab Environm Microbiol Sichuan Prov, Chengdu 610041, Peoples R China

[3] Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromol, Natl Lab Biomacromol, Beijing 100101, Peoples R China

[4] Univ Chinese Acad Sci, Beijing 100049, Peoples R China

来源：

SCIENTIFIC REPORTS | 2017年 / 7卷

基金：

中国国家自然科学基金;

关键词：

ESCHERICHIA-COLI; PRIMER SYNTHESIS; HELICASE; REPLICATION; COMPLEX; DOMAIN; POLYMERASE; SEQUENCE; PROTEIN; IDENTIFICATION;

D O I：

10.1038/s41598-017-00767-8

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Bacterial primase initiates the repeated synthesis of short RNA primers that are extended by DNA polymerase to synthesize Okazaki fragments on the lagging strand at replication forks. It remains unclear how the enzyme recognizes specific initiation sites. In this study, the DnaG primase from Bacillus subtilis (BsuDnaG) was characterized and the crystal structure of the RNA polymerase domain (RPD) was determined. Structural comparisons revealed that the tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. Structural and biochemical data defined the ssDNA template binding surface as an L shape, and a model for the template ssDNA binding to primase is proposed. The flexibility of the DnaG primases from B. subtilis and G. stearothermophilus were compared, and the results implied that the intrinsic flexibility of the primase may facilitate the interactions between primase and various partners in the replisome. These results shed light on the mechanism by which DnaG recognizes the specific initiation site.

引用

页数：8

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