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Published online on March 13, 2001, 10.1073/pnas.061034498
PNAS | April 10, 2001 | vol. 98 | no. 8 | 4569-4574


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Genetics
 A comprehensive two-hybrid analysis to explore the yeast protein interactome

Takashi Ito*,dagger , Tomoko Chiba*, Ritsuko OzawaDagger , Mikio Yoshida§, Masahira HattoriDagger , and Yoshiyuki SakakiDagger ,

* Division of Genome Biology, Cancer Research Institute, Kanazawa University, Kanazawa 920-0934, Japan; Dagger  Human Genome Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan; § INTEC Web and Genome Informatics Corporation, Tokyo 136-0075, Japan; and  Human Genome Center, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan

Communicated by Satoshi Omura, The Kitasato Institute, Tokyo, Japan, January 22, 2001 (received for review December 4, 2000)

Protein-protein interactions play crucial roles in the execution of various biological functions. Accordingly, their comprehensive description would contribute considerably to the functional interpretation of fully sequenced genomes, which are flooded with novel genes of unpredictable functions. We previously developed a system to examine two-hybrid interactions in all possible combinations between the approx 6,000 proteins of the budding yeast Saccharomyces cerevisiae. Here we have completed the comprehensive analysis using this system to identify 4,549 two-hybrid interactions among 3,278 proteins. Unexpectedly, these data do not largely overlap with those obtained by the other project [Uetz, P., et al. (2000) Nature (London) 403, 623-627] and hence have substantially expanded our knowledge on the protein interaction space or interactome of the yeast. Cumulative connection of these binary interactions generates a single huge network linking the vast majority of the proteins. Bioinformatics-aided selection of biologically relevant interactions highlights various intriguing subnetworks. They include, for instance, the one that had successfully foreseen the involvement of a novel protein in spindle pole body function as well as the one that may uncover a hitherto unidentified multiprotein complex potentially participating in the process of vesicular transport. Our data would thus significantly expand and improve the protein interaction map for the exploration of genome functions that eventually leads to thorough understanding of the cell as a molecular system.

dagger To whom reprint requests should be addressed at: Division of Genome Biology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920-0934, Japan. E-mail: titolab{at}kenroku.kanazawa-u.ac.jp.

www.pnas.org/cgi/doi/10.1073/pnas.061034498
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Related Commentary in PNAS:

Networking proteins in yeast
Tony R. Hazbun and Stanley Fields
PNAS 2001 98: 4277-4278. [Extract] [Full Text]  



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