The article "Proteome survey reveals modularity of the yeast cell machinery" will appear on 22 January in the on-line version of Nature.
The paper describes the characterization of nearly 500 protein complexes (the molecular machines of a cell) in the model organism, S. cerevisiae.
The researchers have demonstrated how proteins are organized into core complexes, which recruit other specific proteins dynamically to refine their function, for example in response to external signals, or in different stages of the cell cycle.
The understanding of how proteins come together to form these protein complexes, and on a higher level, how complexes assemble to regulate protein pathways, will potentially enable the elucidation of the molecular basis of health and disease and the identification of appropriate targets for drug discovery in these pathways.
Tim Edwards, CEO of Cellzome said, "I am very proud of our team of scientists and their colleagues at the EMBL. This has been a very fruitful collaboration and the publication in Nature demonstrates the quality of our pathway work."
Rob Russell, Group Leader at EMBL said, "Cellzome certainly has generated a data set of outstanding quality - enabling us to develop and exercise the right computational tools to discover new complexes and define their modular nature. It has been a pleasure to work with Cellzome on this exciting project."
In previous work published in Nature and Nature Cell Biology, Cellzome reported the maps of protein complexes and pathways, most notably the pro-inflammatory Tumor Necrosis Factor alpha (TNFa) signaling pathway.
Cellzome is also applying this technology in a broad collaboration with Novartis for the charting of the physical and functional protein maps of key cellular pathways for the development of drug candidates.