Protein-protein interactions between two-component system transmitter and receiver domains of Myxococcus xanthus.
We present a novel dataset assessing the specificity of protein-protein interactions between 69 transmitter and receiver domains from two-component system (TCS)-signalling pathways. TCS require a conserved protein-protein interaction between partner transmitter and receiver domains for signal transduction. The complex prokaryote Myxococcus xanthus possesses an unusually large number of TCS genes, many of which have no obvious interaction partners. Interactions between TCS domains of M. xanthus were assessed using a yeast two-hybrid assay, in which domains were expressed as both bait and prey translational fusions. LacZ production was monitored as an indicator of protein-protein interaction, and the strength of interactions classified as weak, medium or strong. Two-hundred and fifty-five transmitter-receiver domain interactions were observed (46 strong), allowing identification of potential signalling partners for individual M. xanthus TCS proteins. In addition, the dataset provides interesting 'meta' information. For instance, many strong interactions were identified between different transmitter domain pairs (34) and receiver domain pairs (23), suggesting a surprisingly large degree of heterodimerisation of these domains. Proteins in our dataset that exhibited similar 'profiles' of interactions, often shared a similar biological function, suggesting that interaction profiles can provide information on biological function, even considering sets of homologous domains.
Whitworth
David E
DE
Department of Biological Sciences, University of Warwick, Coventry, UK. d.e.whitworth@warwick.ac.uk
Millard
Andrew
A
Hodgson
David A
DA
Hawkins
Peter F
PF
D001426:Bacterial Proteins / Q000737:chemistry; D016000:Cluster Analysis; D030562:Databases, Protein; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D007763:Lac Operon; D016941:Myxococcus xanthus / Q000378:metabolism*; D014176:Protein Biosynthesis; D025941:Protein Interaction Mapping; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction; D020798:Two-Hybrid System Techniques
D001426:Bacterial Proteins; D020543:Proteome