ArticleScientific reports2016
Conformational plasticity of RepB, the replication initiator protein of promiscuous streptococcal plasmid pMV158.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Evidence ofApplied and environmental microbiology · 2025Article
- Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein.Nucleic acids research · 2023Article
- Functional Analysis of EspM, an ESX-1-Associated Transcription Factor in Mycobacterium marinum.Journal of bacteriology · 2022Article
- A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues.Viruses · 2021Article
- Acidic pH Decreases the Endonuclease Activity of Initiator RepB and Increases the Stability of the Covalent RepB-DNA Intermediate while Has Only a Limited Effect on the Replication of Plasmid pMV158 inFrontiers in molecular biosciences · 2021Article
- RovC - a novel type of hexameric transcriptional activator promoting type VI secretion gene expression.PLoS pathogens · 2020Article
- A specific class of infectious agents isolated from bovine serum and dairy products and peritumoral colon cancer tissue.Emerging microbes & infections · 2019Article
- Successful Establishment of Plasmids R1 and pMV158 in a New Host Requires the Relief of the Transcriptional Repression of Their EssentialFrontiers in microbiology · 2017Article
- The Different Faces of Rolling-Circle Replication and Its Multifunctional Initiator Proteins.Frontiers in microbiology · 2017Review
- Replication of Staphylococcal Resistance Plasmids.Frontiers in microbiology · 2017Review
- Metal-Induced Stabilization and Activation of Plasmid Replication Initiator RepB.Frontiers in molecular biosciences · 2016Article
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Authors and funding
9 authors.
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Abstract
DNA replication initiation is a vital and tightly regulated step in all replicons and requires an initiator factor that specifically recognizes the DNA replication origin and starts replication. RepB from the promiscuous streptococcal plasmid pMV158 is a hexameric ring protein evolutionary related to viral initiators. Here we explore the conformational plasticity of the RepB hexamer by i) SAXS, ii) sedimentation experiments, iii) molecular simulations and iv) X-ray crystallography. Combining these techniques, we derive an estimate of the conformational ensemble in solution showing that the C-terminal oligomerisation domains of the protein form a rigid cylindrical scaffold to which the N-terminal DNA-binding/catalytic domains are attached as highly flexible appendages, featuring multiple orientations. In addition, we show that the hinge region connecting both domains plays a pivotal role in the observed plasticity. Sequence comparisons and a literature survey show that this hinge region could exists in other initiators, suggesting that it is a common, crucial structural element for DNA binding and manipulation.
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