Unknown

Dataset Information

0

Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.


ABSTRACT: 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.

SUBMITTER: Huang YH 

PROVIDER: S-EPMC4129139 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.

Huang Yen-Hua YH   Huang Cheng-Yang CY  

BioMed research international 20140721


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 chr  ...[more]

Similar Datasets

| S-EPMC3910646 | biostudies-literature
| S-EPMC54168 | biostudies-other
| S-EPMC5175346 | biostudies-literature
| S-EPMC6283420 | biostudies-literature
| S-EPMC6331220 | biostudies-literature