ArticleThe Journal of biological chemistry2011
Functional characterization of the multidomain F plasmid TraI relaxase-helicase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Cryo-EM Structure of the relaxosome, a complex essential for bacterial mating and the spread of antibiotic resistance genes.Nature communications · 2025Article
- DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island.Nucleic acids research · 2019Article
- Identification and Characterization ofFrontiers in microbiology · 2019Article
- Unique helicase determinants in the essential conjugative TraI factor from Salmonella enterica serovar Typhimurium plasmid pCU1.Journal of bacteriology · 2014Article
- Structures of TraI in solution.Journal of molecular modeling · 2014Article
- Structure of a translocation signal domain mediating conjugative transfer by type IV secretion systems.Molecular microbiology · 2013Article
- Article
- Crystal structure of the plant epigenetic protein arginine methyltransferase 10.Journal of molecular biology · 2011Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
TraI, a bifunctional enzyme containing relaxase and helicase activities, initiates and drives the conjugative transfer of the Escherichia coli F plasmid. Here, we examined the structure and function of the TraI helicase. We show that TraI binds to single-stranded DNA (ssDNA) with a site size of ∼25 nucleotides, which is significantly longer than the site size of other known superfamily I helicases. Low cooperativity was observed with the binding of TraI to ssDNA, and a double-stranded DNA-binding site was identified within the N-terminal region of TraI 1-858, outside the core helicase motifs of TraI. We have revealed that the affinity of TraI for DNA is negatively correlated with the ionic strength of the solution. The binding of AMPPNP or ADP results in a 3-fold increase in the affinity of TraI for ssDNA. Moreover, TraI prefers to bind ssDNA oligomers containing a single type of base. Finally, we elucidated the solution structure of TraI using small angle x-ray scattering. TraI exhibits an ellipsoidal shape in solution with four domains aligning along one axis. Taken together, these data result in the assembly of a model for the multidomain helicase activity of TraI.
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