PMID:18717787
| Citation |
Lu, J, Wong, JJ, Edwards, RA, Manchak, J, Frost, LS and Glover, JN (2008) Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation. Mol. Microbiol. 70:89-99 |
|---|---|
| Abstract |
F plasmid-mediated bacterial conjugation requires interactions between a relaxosome component, TraM, and the coupling protein TraD, a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore. Here we present the crystal structure of the C-terminal tail of TraD bound to the TraM tetramerization domain, the first structural evidence of relaxosome-coupling protein interactions. The structure reveals the TraD C-terminal peptide bound to each of four symmetry-related grooves on the surface of the TraM tetramer. Extensive protein-protein interactions were observed between the two proteins. Mutational analysis indicates that these interactions are specific and required for efficient F conjugation in vivo. Our results suggest that specific interactions between the C-terminal tail of TraD and the TraM tetramerization domain might lead to more generalized interactions that stabilize the relaxosome-coupling protein complex in preparation for conjugative DNA transfer. |
| Links |
PubMed Online version:10.1111/j.1365-2958.2008.06391.x |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Conjugation, Genetic; DNA, Bacterial/genetics; Escherichia coli/genetics; Escherichia coli Proteins/genetics; F Factor/genetics; Membrane Proteins/genetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Promoter Regions, Genetic; Protein Interaction Domains and Motifs; Sequence Alignment |
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