ArticleBiochemistry2014
Crystal structures of the F and pSLT plasmid TraJ N-terminal regions reveal similar homodimeric PAS folds with functional interchangeability.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Comprehensive analysis of Enterobacteriaceae IncX plasmids reveals robust conjugation regulators PrfaH, H-NS, and conjugation-fitness tradeoff.Communications biology · 2025Article
- Article
- Protein Dynamics in F-like Bacterial Conjugation.Biomedicines · 2020Review
- Regulation of R1 Plasmid Transfer by H-NS, ArcA, TraJ, and DNA Sequence Elements.Frontiers in microbiology · 2020Article
- Cooperative Function of TraJ and ArcA in Regulating the F PlasmidJournal of bacteriology · 2019Article
- Spread and Persistence of Virulence and Antibiotic Resistance Genes: A Ride on the F Plasmid Conjugation Module.EcoSal Plus · 2018Review
- Comparative Genomics of the Conjugation Region of F-like Plasmids: Five Shades of F.Frontiers in molecular biosciences · 2016Article
- Article
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Authors and funding
5 authors.
Funding
Abstract
In the F family of conjugative plasmids, TraJ is an essential transcriptional activator of the tra operon that encodes most of the proteins required for conjugation. Here we report for the first time the X-ray crystal structures of the TraJ N-terminal domains from the prototypic F plasmid (TraJF(11-130)) and from the Salmonella virulence plasmid pSLT (TraJpSLT(1-128)). Both structures contain similar Per-ARNT-Sim (PAS) folds, which further homodimerize through the N-terminal helix and the structurally conserved β-sheet of the PAS fold from each protomer. Mutational analysis reveals that the observed dimeric interface is critical for TraJF transcriptional activation, indicating that dimerization of TraJ is required for its in vivo function. TraJ is specific in activating its cognate tra operon promoter; however, heterologous PAS domains from pSLT and R100 TraJ can functionally replace the TraJF PAS domain, suggesting that the allelic specificity of TraJ is solely mediated by the region C-terminal to the PAS domain.
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