ArticleMolecular microbiology2019
Cryptic protein interactions regulate DNA replication initiation.
Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Bacillus subtilis DnaB forms multiple protein-protein interactions essential for DNA replication initiation.Nucleic acids research · 2026Article
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- SirA inhibits the essential DnaA:DnaD interaction to block helicase recruitment during Bacillus subtilis sporulation.Nucleic acids research · 2023Article
- Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.Journal of bacteriology · 2023Review
- Structure and kinase activity of bacterial cell cycle regulator CcrZ.PLoS genetics · 2022Article
- DNA damage checkpoint activation affects peptidoglycan synthesis and late divisome components in Bacillus subtilis.Molecular microbiology · 2021Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- Identification of a basal system for unwinding a bacterial chromosome origin.The EMBO journal · 2019Article
- DNA replication initiation in Bacillus subtilis: structural and functional characterization of the essential DnaA-DnaD interaction.Nucleic acids research · 2019Article
- Discovery of a dual protease mechanism that promotes DNA damage checkpoint recovery.PLoS genetics · 2018Article
- Molecular insights into replication initiation in a multipartite genome harboring bacterium Deinococcus radiodurans.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
DNA replication is a fundamental biological process that is tightly regulated in all cells. In bacteria, DnaA controls when and where replication begins by building a step-wise complex that loads the replicative helicase onto chromosomal DNA. In many low-GC Gram-positive species, DnaA recruits the DnaD and DnaB proteins to function as adaptors to assist in helicase loading. How DnaA, its adaptors and the helicase form a complex at the origin is unclear. We addressed this question using the bacterial two-hybrid assay to determine how the initiation proteins from Bacillus subtilis interact with each other. We show that cryptic interaction sites play a key role in this process and we map these regions for the entire pathway. In addition, we found that the SirA regulator that blocks initiation in sporulating cells binds to a surface on DnaA that overlaps with DnaD. The interaction between DnaA and DnaD was also mapped to the same DnaA surface in the human pathogen Staphylococcus aureus, demonstrating the broad conservation of this surface. Therefore, our study has unveiled key protein interactions essential for initiation and our approach is widely applicable for mapping interactions in other signaling pathways that are governed by cryptic binding surfaces.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.