ArticleThe protein journal2013
Yeast two-hybrid analysis of PriB-interacting proteins in replication restart primosome: a proposed PriB-SSB interaction model.
Article in The protein journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- The intrinsically disordered linker in the single-stranded DNA-binding protein influences DNA replication restart and recombination pathways inJournal of bacteriology · 2024Article
- The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.Antibiotics (Basel, Switzerland) · 2018Review
- Mechanisms of bacterial DNA replication restart.Nucleic acids research · 2018Review
- Structure and Function of the PriC DNA Replication Restart Protein.The Journal of biological chemistry · 2016Article
- Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.BioMed research international · 2014Article
- Molecular insights into the prototypical single-stranded DNA-binding protein fromCritical reviews in biochemistry and molecular biologyReview
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PriB is one of the components of the replication restart primosome. The activity mediated by the primosomal proteins, including PriB, is required for reinitiating chromosomal DNA replication in bacteria after DNA damage. As such, the study of the interactions between PriB and members in the primosome is essential to better understand their mechanism of action. In this study, we investigated PriB-interacting proteins in the primosome through the yeast two-hybrid system. Yeast two-hybrid analysis using two strains, Y187 and AH109, revealed that PriB interacts with PriA, DnaT, SSB, and itself and does not interact with DnaA, DnaB, DnaC, or DnaG. In addition, mutational analysis showed that PriB may bind to SSB via K82, K84, and K89 in the L(45) loop. Based on these preliminary data, we proposed a PriB-SSB interaction model. Further work can focus on determination of how PriB binds to the PriA-SSB complex in replication restart.
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Registered trials
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