Structure and Function of the PriC DNA Replication Restart Protein
文献类型：期刊论文
| 作者 | Wessel, Sarah R.1; Cornilescu, Claudia C.2,3; Cornilescu, Gabriel2,3; Metz, Alice4; Leroux, Maxime4; Hu, Kaifeng2,3,5 ; Sandler, Steven J.4; Markley, John L.2,3; Keck, James L.1
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| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
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| 出版日期 | 2016-08-26 |
| 卷号 | 291期号:35页码:18384-18396 |
| 关键词 | DNA helicase DNA replication DNA-protein interaction nuclear magnetic resonance (NMR) protein-protein interaction DNA replication restart DnaB helicase PriC single-stranded DNA-binding protein |
| 英文摘要 | Collisions between DNA replication complexes (replisomes) and barriers such as damaged DNA or tightly bound protein complexes can dissociate replisomes from chromosomes prematurely. Replisomes must be reloaded under these circumstances to avoid incomplete replication and cell death. Bacteria have evolved multiple pathways that initiate DNA replication restart by recognizing and remodeling abandoned replication forks and reloading the replicative helicase. In vitro, the simplest of these pathways is mediated by the single-domain PriC protein, which, along with the DnaC helicase loader, can load the DnaB replicative helicase onto DNA bound by the single-stranded DNA (ssDNA)-binding protein (SSB). Previous biochemical studies have identified PriC residues that mediate interactions with ssDNA and SSB. However, the mechanisms by which PriC drives DNA replication restart have remained poorly defined due to the limited structural information available for PriC. Here, we report the NMR structure of full-length PriC from Cronobacter sakazakii. PriC forms a compact bundle of -helices that brings together residues involved in ssDNA and SSB binding at adjacent sites on the protein surface. Disruption of these interaction sites and of other conserved residues leads to decreased DnaB helicase loading onto SSB-bound DNA. We also demonstrate that PriC can directly interact with DnaB and the DnaB |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | N-TERMINAL DOMAIN ; ESCHERICHIA-COLI ; BINDING PROTEIN ; PRIMOSOME FACTOR ; FORKS ; INITIATION ; COMPLEX ; POLYMERASE ; HELICASE ; DYNAMICS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000383241800029 |
| 源URL | [http://ir.kib.ac.cn/handle/151853/28641]  |
| 专题 | 昆明植物研究所_植物化学与西部植物资源持续利用国家重点实验室 |
| 作者单位 | 1.Univ Wisconsin, Sch Med & Publ Hlth, Dept Biomol Chem, 1135 Biochem Sci Bldg,420 Henry Mall, Madison, WI 53706 USA 2.Univ Wisconsin, Natl Magnet Resonance Facil Madison, Madison, WI 53706 USA 3.Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA 4.Univ Massachusetts, Dept Microbiol, Amherst, MA 01003 USA 5.Chinese Acad Sci, Kunming Inst Bot, State Key Lab Phytochem & Plant Resources West Ch, Grp Liquid State NMR, Kunming 650201, Yunnan, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wessel, Sarah R.,Cornilescu, Claudia C.,Cornilescu, Gabriel,et al. Structure and Function of the PriC DNA Replication Restart Protein[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(35):18384-18396. |
| APA | Wessel, Sarah R..,Cornilescu, Claudia C..,Cornilescu, Gabriel.,Metz, Alice.,Leroux, Maxime.,...&Keck, James L..(2016).Structure and Function of the PriC DNA Replication Restart Protein.JOURNAL OF BIOLOGICAL CHEMISTRY,291(35),18384-18396. |
| MLA | Wessel, Sarah R.,et al."Structure and Function of the PriC DNA Replication Restart Protein".JOURNAL OF BIOLOGICAL CHEMISTRY 291.35(2016):18384-18396. |
入库方式： OAI收割
来源：昆明植物研究所
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