Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT

被引:89
作者
Huang, Yen-Hua [1 ]
Huang, Cheng-Yang [1 ,2 ]
机构
[1] Chung Shan Med Univ, Sch Biomed Sci, Taichung 40201, Taiwan
[2] Chung Shan Med Univ Hosp, Dept Med Res, Taichung 40201, Taiwan
关键词
STALLED REPLICATION FORKS; PHI X174-TYPE PRIMOSOME; N-TERMINAL DOMAIN; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; HEXAMERIC HELICASE; RESTART PRIMOSOME; COMPLEX-FORMATION; LAGGING-STRAND; OB-FOLD;
D O I
10.1155/2014/195162
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Replication restart primosome is a complex dynamic system that is essential for bacterial survival. This system uses various proteins to reinitiate chromosomal DNA replication to maintain genetic integrity after DNA damage. The replication restart primosome in Escherichia coli is composed of PriA helicase, PriB, PriC, DnaT, DnaC, DnaB helicase, and DnaG primase. The assembly of the protein complexes within the forked DNA responsible for reloading the replicative DnaB helicase anywhere on the chromosome for genome duplication requires the coordination of transient biomolecular interactions. Over the last decade, investigations on the structure and mechanism of these nucleoproteins have provided considerable insight into primosome assembly. In this review, we summarize and discuss our current knowledge and recent advances on the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
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页数:14
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