ArticleNucleic acids research2011
The MobM relaxase domain of plasmid pMV158: thermal stability and activity upon Mn2+ and specific DNA binding.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Performance of the pBHR1 mobilization protein MobV and its role in stable plasmid expression inMicrobiology spectrum · 2026Article
- Exploration of DNA processing features unravels novel properties of ICE conjugation in Gram-positive bacteria.Nucleic acids research · 2022Article
- Recognition of Streptococcal Promoters by the Pneumococcal SigA Protein.Frontiers in molecular biosciences · 2021Article
- Regulation of Gram-Positive Conjugation.Frontiers in microbiology · 2019Review
- Characterization of a relaxase belonging to the MOBMobile DNA · 2019Article
- DNA structure at the plasmid origin-of-transfer indicates its potential transfer range.Scientific reports · 2018Article
- Relaxase MobM Induces a Molecular Switch at Its Cognate Origin of Transfer.Frontiers in molecular biosciences · 2018Article
- Structural basis of a histidine-DNA nicking/joining mechanism for gene transfer and promiscuous spread of antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Crosstalk between vertical and horizontal gene transfer: plasmid replication control by a conjugative relaxase.Nucleic acids research · 2017Article
- The Different Faces of Rolling-Circle Replication and Its Multifunctional Initiator Proteins.Frontiers in microbiology · 2017Review
- Streptococcal group B integrative and mobilizable element IMESag-rpsI encodes a functional relaxase involved in its transfer.Open biology · 2016Article
- Metal-Induced Stabilization and Activation of Plasmid Replication Initiator RepB.Frontiers in molecular biosciences · 2016Article
- Mobilizable Rolling-Circle Replicating Plasmids from Gram-Positive Bacteria: A Low-Cost Conjugative Transfer.Microbiology spectrum · 2014Article
- Bringing them together: plasmid pMV158 rolling circle replication and conjugation under an evolutionary perspective.Plasmid · 2014Review
- Functional properties and structural requirements of the plasmid pMV158-encoded MobM relaxase domain.Journal of bacteriology · 2013Article
- Autoregulation of the synthesis of the MobM relaxase encoded by the promiscuous plasmid pMV158.Journal of bacteriology · 2012Article
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6 authors.
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Abstract
Protein MobM, the relaxase involved in conjugative transfer of the streptococcal plasmid pMV158, is the prototype of the MOB(V) superfamily of relaxases. To characterize the DNA-binding and nicking domain of MobM, a truncated version of the protein (MobMN199) encompassing its N-terminal region was designed and the protein was purified. MobMN199 was monomeric in contrast to the dimeric form of the full-length protein, but it kept its nicking activity on pMV158 DNA. The optimal relaxase activity was dependent on Mn(2+) or Mg(2+) cations in a dosage-dependent manner. However, whereas Mn(2+) strongly stabilized MobMN199 against thermal denaturation, no protective effect was observed for Mg(2+). Furthermore, MobMN199 exhibited a high affinity binding for Mn(2+) but not for Mg(2+). We also examined the binding-specificity and affinity of MobMN199 for several substrates of single-stranded DNA encompassing the pMV158 origin of transfer (oriT). The minimal oriT was delimited to a stretch of 26 nt which included an inverted repeat located eight bases upstream of the nick site. The structure of MobMN199 was strongly stabilized by binding to the defined target DNA, indicating the formation of a tight protein-DNA complex. We demonstrate that the oriT recognition by MobMN199 was highly specific and suggest that this protein most probably employs Mn(2+) during pMV158 transfer.
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