Editors' ChoiceProteomics

Brewing Up Something Special in Yeast

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Science's STKE  15 Feb 2000:
Vol. 2000, Issue 19, pp. tw7
DOI: 10.1126/stke.2000.19.tw7

As a consequence of sequencing whole genomes and identifying all potential open reading frames, scientists face the daunting task of determining the functions of proteins coded by each genome. Whether by immunoprecipitation or the yeast two hybrid method, coassociation with proteins of known function can provide clues to the functional identification of novel proteins and their placement within specific pathways. Uetz et al. have undertaken the enormous task of identifying protein-protein associations among the approximately 6,000 proteins expressed in Saccharomyces cerevisiae. The authors employed a two-prong approach to yeast proteomics utilizing array screening and library screening. These powerful screening techniques revealed functions for two novel proteins in arginine metabolism; a new cell cycle regulatory role for the cyclin-dependent kinase Cks1 through its interactions with three cyclinB proteins; novel interactions between proteins known to be involved in RNA splicing; and linking of proteins known to perform discrete functions such as double-strand DNA break formation and crossover resolution into the larger biological context of meiotic recombination via a protein common to both activities. In an accompanying News & Views perspective, Oliver discusses the importance of screening approaches, and provides details on the techniques used by Uetz et al.

Oliver, S. Guilt-by-association goes global. (2000) Nature 403: 601. [Online Journal]

Uetz, P., Giot, L., Cagney, G., Mansfield, T.A., Judson, R.S., Knight, J.R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., Qureshi-Emili, A., Li, Y., Godwin, B., Conover, D., Kalbfleisch, T.,Vijayadamodar, G., Yang, M., Johnston, M., Fields, S., and Rothberg, J. M. (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403: 623-627. [Online Journal]

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