ArticleBiomolecular NMR assignments2011
Chemical shift assignments for F-plasmid TraI (381-569).
Article in Biomolecular NMR assignments, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
4 citing papers in PubMed, 5 citations in OpenAlex.
- Biophysical characterization of naturally occurring titin M10 mutations.Protein science : a publication of the Protein Society · 2015Article
- Structures of TraI in solution.Journal of molecular modeling · 2014Article
- Article
- An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation.Molecular microbiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
TraI, the F plasmid-encoded nickase, is a 1,756 amino acid protein essential for conjugative transfer of F plasmid DNA from one bacterium to another. While crystal structures of N- and C-terminal domains of F TraI have been determined, central domains of the protein are structurally unexplored. These middle domains (between residues 306 and 1,500) are known to both bind single-stranded DNA (ssDNA) and unwind DNA through a highly processive helicase activity. Of this central region, the more C-terminal portion (~900-1500) appears related to helicase RecD of the E. coli RecBCD complex. The more N-terminal portion (306-900), however, shows limited sequence similarity to other proteins. In an attempt to define the structure of well-folded domains of this middle region and discern their function, we have isolated stable regions of TraI following limited proteolysis. One of these regions, TraI (381-569), was identified and a genetic construct encoding it was engineered. The protein was expressed, purified, and the sequence-specific chemical shifts for it were assigned.
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Registered trials
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