ArticleProceedings of the National Academy of Sciences of the United States of America2014
Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 49 citations in OpenAlex.
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- CanFrontiers in cellular and infection microbiology · 2025Article
- Search for Origins of Anti-CRISPR Proteins by Structure Comparison.The CRISPR journal · 2023Article
- SirA inhibits the essential DnaA:DnaD interaction to block helicase recruitment during Bacillus subtilis sporulation.Nucleic acids research · 2023Article
- Whole-Genome Sequence of Multidrug-Resistant Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2022Article
- The loopometer: a quantitative in vivo assay for DNA-looping proteins.Nucleic acids research · 2021Article
- Thousands of previously unknown phages discovered in whole-community human gut metagenomes.Microbiome · 2021Article
- Genome replication dynamics of a bacteriophage and its satellite reveal strategies for parasitism and viral restriction.Nucleic acids research · 2020Article
- Structural analysis of a replication protein encoded by a plasmid isolated from a multiple sclerosis patient.Acta crystallographica. Section D, Structural biology · 2019Article
- Enterococcal Genetics.Microbiology spectrum · 2019Review
- Cryptic protein interactions regulate DNA replication initiation.Molecular microbiology · 2019Article
- Staphylococcal Plasmids, Transposable and Integrative Elements.Microbiology spectrum · 2018Review
- Structural analyses of the bacterial primosomal protein DnaB reveal that it is a tetramer and forms a complex with a primosomal re-initiation protein.The Journal of biological chemistry · 2017Article
- New Macrolide-Lincosamide-Streptogramin B Resistance GeneAntimicrobial agents and chemotherapy · 2017Article
- Plasmid Replicons fromFrontiers in microbiology · 2017Article
- Replication of Staphylococcal Resistance Plasmids.Frontiers in microbiology · 2017Review
- Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016Review
- Structural basis for replication origin unwinding by an initiator primase of plasmid ColE2-P9: duplex DNA unwinding by a single protein.The Journal of biological chemistry · 2015Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The staphylococcal multiresistance plasmids are key contributors to the alarming rise in bacterial multidrug resistance. A conserved replication initiator, RepA, encoded on these plasmids is essential for their propagation. RepA proteins consist of flexibly linked N-terminal (NTD) and C-terminal (CTD) domains. Despite their essential role in replication, the molecular basis for RepA function is unknown. Here we describe a complete structural and functional dissection of RepA proteins. Unexpectedly, both the RepA NTD and CTD show similarity to the corresponding domains of the bacterial primosome protein, DnaD. Although the RepA and DnaD NTD both contain winged helix-turn-helices, the DnaD NTD self-assembles into large scaffolds whereas the tetrameric RepA NTD binds DNA iterons using a newly described DNA binding mode. Strikingly, structural and atomic force microscopy data reveal that the NTD tetramer mediates DNA bridging, suggesting a molecular mechanism for origin handcuffing. Finally, data show that the RepA CTD interacts with the host DnaG primase, which binds the replicative helicase. Thus, these combined data reveal the molecular mechanism by which RepA mediates the specific replicon assembly of staphylococcal multiresistant plasmids.
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