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

Abstract 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 fro...

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Autores principales:	Yingqin Zhou, Hao Luo, Zhongchuan Liu, Mu Yang, Xiaoyun Pang, Fei Sun, Ganggang Wang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7e31cef1246f454da01f4bd8e2ead46a
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spelling	oai:doaj.org-article:7e31cef1246f454da01f4bd8e2ead46a2021-12-02T16:07:58ZStructural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria10.1038/s41598-017-00767-82045-2322https://doaj.org/article/7e31cef1246f454da01f4bd8e2ead46a2017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00767-8https://doaj.org/toc/2045-2322Abstract 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.Yingqin ZhouHao LuoZhongchuan LiuMu YangXiaoyun PangFei SunGanggang WangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yingqin Zhou Hao Luo Zhongchuan Liu Mu Yang Xiaoyun Pang Fei Sun Ganggang Wang Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
description	Abstract 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.
format	article
author	Yingqin Zhou Hao Luo Zhongchuan Liu Mu Yang Xiaoyun Pang Fei Sun Ganggang Wang
author_facet	Yingqin Zhou Hao Luo Zhongchuan Liu Mu Yang Xiaoyun Pang Fei Sun Ganggang Wang
author_sort	Yingqin Zhou
title	Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
title_short	Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
title_full	Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
title_fullStr	Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
title_full_unstemmed	Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
title_sort	structural insight into the specific dna template binding to dnag primase in bacteria
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7e31cef1246f454da01f4bd8e2ead46a
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_version_	1718384665761415168

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

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