ArticleNucleic acids research2010
The mechanism and control of DNA transfer by the conjugative relaxase of resistance plasmid pCU1.
Article in Nucleic acids research, 2010. 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.
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- Structural and functional characterization of TraI from pKM101 reveals basis for DNA processing.Life science alliance · 2023Article
- The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.Molecular cell · 2021Article
- DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island.Nucleic acids research · 2019Article
- Characterization of a relaxase belonging to the MOBMobile DNA · 2019Article
- 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
- Orthogonal Protein Assembly on DNA Nanostructures Using Relaxases.Angewandte Chemie (International ed. in English) · 2016Article
- Article
- Metal-Induced Stabilization and Activation of Plasmid Replication Initiator RepB.Frontiers in molecular biosciences · 2016Article
- Origin-of-transfer sequences facilitate mobilisation of non-conjugative antimicrobial-resistance plasmids in Staphylococcus aureus.Nucleic acids research · 2015Article
- Unique helicase determinants in the essential conjugative TraI factor from Salmonella enterica serovar Typhimurium plasmid pCU1.Journal of bacteriology · 2014Article
- A high security double lock and key mechanism in HUH relaxases controls oriT-processing for plasmid conjugation.Nucleic acids research · 2014Article
- Breaking and joining single-stranded DNA: the HUH endonuclease superfamily.Nature reviews. Microbiology · 2013Review
- Functional properties and structural requirements of the plasmid pMV158-encoded MobM relaxase domain.Journal of bacteriology · 2013Article
- Molecular basis of antibiotic multiresistance transfer in Staphylococcus aureus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Investigating the impact of bisphosphonates and structurally related compounds on bacteria containing conjugative plasmids.Biochemical and biophysical research communications · 2012Article
- The MobM relaxase domain of plasmid pMV158: thermal stability and activity upon Mn2+ and specific DNA binding.Nucleic acids research · 2011Article
- Tyrosine partners coordinate DNA nicking by the Salmonella typhimurium plasmid pCU1 relaxase enzyme.FEBS letters · 2011Article
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5 authors.
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Abstract
Bacteria expand their genetic diversity, spread antibiotic resistance genes, and obtain virulence factors through the highly coordinated process of conjugative plasmid transfer (CPT). A plasmid-encoded relaxase enzyme initiates and terminates CPT by nicking and religating the transferred plasmid in a sequence-specific manner. We solved the 2.3 A crystal structure of the relaxase responsible for the spread of the resistance plasmid pCU1 and determined its DNA binding and nicking capabilities. The overall fold of the pCU1 relaxase is similar to that of the F plasmid and plasmid R388 relaxases. However, in the pCU1 structure, the conserved tyrosine residues (Y18,19,26,27) that are required for DNA nicking and religation were displaced up to 14 A out of the relaxase active site, revealing a high degree of mobility in this region of the enzyme. In spite of this flexibility, the tyrosines still cleaved the nic site of the plasmid's origin of transfer, and did so in a sequence-specific, metal-dependent manner. Unexpectedly, the pCU1 relaxase lacked the sequence-specific DNA binding previously reported for the homologous F and R388 relaxase enzymes, despite its high sequence and structural similarity with both proteins. In summary, our work outlines novel structural and functional aspects of the relaxase-mediated conjugative transfer of plasmid pCU1.
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