ArticleMolecular microbiology2014
Structure and interactions of the Bacillus subtilis sporulation inhibitor of DNA replication, SirA, with domain I of DnaA.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Bacillus subtilis DnaB forms multiple protein-protein interactions essential for DNA replication initiation.Nucleic acids research · 2026Article
- Structures of DnaA domain I reveal a dimer conserved across Actinomycetes.Nucleic acids research · 2026Article
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- Article
- SirA inhibits the essential DnaA:DnaD interaction to block helicase recruitment during Bacillus subtilis sporulation.Nucleic acids research · 2023Article
- A new role for monomeric ParA/Soj in chromosome dynamics in Bacillus subtilis.MicrobiologyOpen · 2023Article
- The LH-DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders.Acta crystallographica. Section D, Structural biology · 2023Article
- HBsu Is Required for the Initiation of DNA Replication in Bacillus subtilis.Journal of bacteriology · 2022Article
- DciA Helicase Operators Exhibit Diversity across Bacterial Phyla.Journal of bacteriology · 2022Article
- Structure and kinase activity of bacterial cell cycle regulator CcrZ.PLoS genetics · 2022Article
- Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase.Nucleic acids research · 2021Article
- A nucleotide-dependent oligomerization of the Escherichia coli replication initiator DnaA requires residue His136 for remodeling of the chromosomal origin.Nucleic acids research · 2020Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- DNA replication initiation in Bacillus subtilis: structural and functional characterization of the essential DnaA-DnaD interaction.Nucleic acids research · 2019Article
- Cryptic protein interactions regulate DNA replication initiation.Molecular microbiology · 2019Article
- DNA gyrase activity regulates DnaA-dependent replication initiation in Bacillus subtilis.Molecular microbiology · 2018Article
- Phosphorylation of theFrontiers in microbiology · 2018Article
- Rv0004 is a new essential member of the mycobacterial DNA replication machinery.PLoS genetics · 2017Article
- Cell Death Pathway That Monitors Spore Morphogenesis.Trends in microbiology · 2017Review
- Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Chromosome copy number in cells is controlled so that the frequency of initiation of DNA replication matches that of cell division. In bacteria, this is achieved through regulation of the interaction between the initiator protein DnaA and specific DNA elements arrayed at the origin of replication. DnaA assembles at the origin and promotes DNA unwinding and the assembly of a replication initiation complex. SirA is a DnaA-interacting protein that inhibits initiation of replication in diploid Bacillus subtilis cells committed to the developmental pathway leading to formation of a dormant spore. Here we present the crystal structure of SirA in complex with the N-terminal domain of DnaA revealing a heterodimeric complex. The interacting surfaces of both proteins are α-helical with predominantly apolar side-chains packing in a hydrophobic interface. Site-directed mutagenesis experiments confirm the importance of this interface for the interaction of the two proteins in vitro and in vivo. Localization of GFP-SirA indicates that the protein accumulates at the replisome in sporulating cells, likely through a direct interaction with DnaA. The SirA interacting surface of DnaA corresponds closely to the HobA-interacting surface of DnaA from Helicobacter pylori even though HobA is an activator of DnaA and SirA is an inhibitor.
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