ArticleJournal of bacteriology2001
Mobilization function of the pBHR1 plasmid, a derivative of the broad-host-range plasmid pBBR1.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 80 citations in OpenAlex.
- Performance of the pBHR1 mobilization protein MobV and its role in stable plasmid expression inMicrobiology spectrum · 2026Article
- A versatile dual-color bacterial reporter system highlights two distinctApplied and environmental microbiology · 2026Article
- Cell-selective multiplexed bioorthogonal noncanonical amino acid tagging for nascent proteomics.Nature chemical biology · 2026Article
- Development of a sensor for disulfide bond formation in diverse bacteria.Journal of bacteriology · 2024Article
- Cloning and expression of Burkholderia polyyne biosynthetic gene clusters in Paraburkholderia hosts provides a strategy for biopesticide development.Microbial biotechnology · 2022Article
- Pathogen-Specific Bactericidal Method Mediated by Conjugative Delivery of CRISPR-Cas13a Targeting Bacterial Endogenous Transcripts.Microbiology spectrum · 2022Article
- A versatile TnPlant communications · 2022Article
- Evaluation of two transformation protocols and screening of positive plasmid introduction into Bacillus cereus EB2, a gram-positive bacterium using qualitative analyses.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Article
- Improved bacterial recombineering by parallelized protein discovery.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Exploring the genome of Arctic Psychrobacter sp. DAB_AL32B and construction of novel Psychrobacter-specific cloning vectors of an increased carrying capacity.Archives of microbiology · 2019Article
- Transfer of a mobile Staphylococcus saprophyticus plasmid isolated from fermented seafood that confers tetracycline resistance.PloS one · 2019Article
- Instability of the 16S rRNA methyltransferase-encoding npmA gene: why have bacterial cells possessing npmA not spread despite their high and broad resistance to aminoglycosides?The Journal of antibiotics · 2018Article
- DNA structure at the plasmid origin-of-transfer indicates its potential transfer range.Scientific reports · 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
- PhaR, a Negative Regulator of PhaP, Modulates the Colonization of a Burkholderia Gut Symbiont in the Midgut of the Host Insect, Riptortus pedestris.Applied and environmental microbiology · 2017Article
- Perturbation of the two-component signal transduction system, BprRS, results in attenuated virulence and motility defects in Burkholderia pseudomallei.BMC genomics · 2016Article
- DNA-Binding Proteins Regulating pIP501 Transfer and Replication.Frontiers in molecular biosciences · 2016Review
- Insect's intestinal organ for symbiont sorting.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The Burkholderia pseudomallei Proteins BapA and BapC Are Secreted TTSS3 Effectors and BapB Levels Modulate Expression of BopE.PloS one · 2015Article
- Regulation of arsenite oxidation by the phosphate two-component system PhoBR in Halomonas sp. HAL1.Frontiers in microbiology · 2015Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The pBHR1 plasmid is a derivative of the small (2.6-kb), mobilizable broad-host-range plasmid pBBR1, which was isolated from the gram-negative bacterium Bordetella bronchiseptica (R. Antoine and C. Locht, Mol. Microbiol. 6:1785-1799, 1992). Plasmid pBBR1 consists of two functional cassettes and presents sequence similarities with the transfer origins of several plasmids and mobilizable transposons from gram-positive bacteria. We show that the Mob protein specifically recognizes a 52-bp sequence which contains, in addition to the transfer origin, the promoter of the mob gene. We demonstrate that this gene is autoregulated. The binding of the Mob protein to the 52-bp sequence could thus allow the formation of a protein-DNA complex with a double function: relaxosome formation and mob gene regulation. We show that the Mob protein is a relaxase, and we located the nic site position in vitro. After sequence alignment, the position of the nic site of pBBR1 corresponds with those of the nick sites of the Bacteroides mobilizable transposon Tn4555 and the streptococcal plasmid pMV158. The oriT of the latter is characteristic of a family of mobilizable plasmids that are found in gram-positive bacteria and that replicate by the rolling-circle mechanism. Plasmid pBBR1 thus appears to be a new member of this group, even though it resides in gram-negative bacteria and does not replicate via a rolling-circle mechanism. In addition, we identified two amino acids of the Mob protein necessary for its activity, and we discuss their involvement in the mobilization mechanism.
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