Although the S. cerevisiae genome sequence was completed in 1996, over 2000 of the protein products encoded by the 6000 yeast genes are yet to be functionally characterized.
Dr. Snyder and colleagues have taken the next step in this post-genomic era: large scale analysis of the proteins encoded by the genome - the proteome. Although the genome sequence provided vast arrays of genetic information, it provided only limited information about how the dynamic nature of the encoded protein products drives cellular processes.
All proteins (with the exception of some mitochondrial and chloroplast proteins) are synthesized on ribosomes in the cytosol, but depending upon their function, the proteins are transported to their specific place of action. Since subcellular localization is a strong indicator of protein function, Dr. Snyder and colleagues developed a high-throughput method to tag individual proteins and visualize their movements within living cells.
Dr. Snyder and colleagues successfully determined the subcellular localization of over 2700 yeast proteins. Using a combination of various approaches, including a statistical computer algorithm, the researchers were able to predict the localization of all 6100 yeast proteins. In doing so, Dr. Snyder and colleagues have provided insight into the potential function of nearly half of all previously uncharacterized yeast proteins.
This work represents a major advance in S. cerevisiae proteomics, but it promises to be just the tip of the iceberg in these post-genomic times.
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Contact: Nora Poppito
poppito@cshl.org
Cold Spring Harbor Laboratory
14-Mar-2002