The first demonstration of a highly accurate, genome-wide method for detecting stable protein-protein interactions, without the requirement for genetic manipulation of the organism (prior tagless methodologies have false discovery rates of >85%).
Combined with our study of protein complexes published in February 2016, which was based on affinity purification coupled with mass spectroscopy (AP-MS), this experiment yielded a more complete picture of the stable protein interactome of the model sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough, further enabling evidence-based annotation of gene function.
Shatsky M, Dong M, Liu H, Yang LL, Choi M, Singer ME, Geller JT, Fisher SJ, Hall SC, Hazen TC, Brenner SE, Butland GP, Jin J, Witkowska HE, Chandonia JM, Biggin MD. (2016) Quantitative tagless co-purification: a method to validate and identify protein-protein interactions. Molecular and Cellular Proteomics. 2016 Apr 20. doi:10.1074/mcp.M115.057117.