The cover story of the 10 January 2002 issue of Nature describes work in the advancing field of proteonmics, the cataloging and functional analysis of the suite of proteins that operate inside an organismís cells. The subject of the report is a pioneering study describing the first draft of a functional map of the yeast proteome. The map visualizes an entire network of protein complexes and their interactions in yeast Saccharomyces cerevisae, forming a basis for the operative organization underlying a cellís activity under different conditions.
The map, developed by a team of scientists from the biotechnology start-up company CellZome and the European Molecular Biology Laboratory (EMBL), is the first of its kind. The map characterizes the function and interactions of 1,440 yeast proteins comprising 232 multi-protein assemblies, or complexes, which directly affect biological activity.
Interestingly, the EMBL press release describes the work as a large-scale study of the ìmolecular machinesî formed by nearly two thousand proteins in a living cell, including the discovery of over a hundred new protein machines, ranging in size from two to eighty-three molecules (The EMBL press release is also available as a nicely-illustrated 5-page Acrobat PDF document). The Cellzome AG press release emphasizes the work as a major step towards transforming information from genome projects into applications such as the discovery of new drugs.
Yet another perspective is available in an article on the Nature Science Update website ("Proteome reveals promiscuity", by Helen Pearson, 10 January 2002).
