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Originally published in Science Express on 26 July 2001
Science 14 September 2001:
Vol. 293. no. 5537, pp. 2101 - 2105
DOI: 10.1126/science.1062191
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Reports

Global Analysis of Protein Activities Using Proteome Chips

Heng Zhu,1 Metin Bilgin,1 Rhonda Bangham,1 David Hall,2 Antonio Casamayor,1 Paul Bertone,1 Ning Lan,2 Ronald Jansen,2 Scott Bidlingmaier,2 Thomas Houfek,3 Tom Mitchell,3 Perry Miller,4 Ralph A. Dean,3 Mark Gerstein,2 Michael Snyder12*

To facilitate studies of the yeast proteome, we cloned 5800 open reading frames and overexpressed and purified their corresponding proteins. The proteins were printed onto slides at high spatial density to form a yeast proteome microarray and screened for their ability to interact with proteins and phospholipids. We identified many new calmodulin- and phospholipid-interacting proteins; a common potential binding motif was identified for many of the calmodulin-binding proteins. Thus, microarrays of an entire eukaryotic proteome can be prepared and screened for diverse biochemical activities. The microarrays can also be used to screen protein-drug interactions and to detect posttranslational modifications.

1 Department of Molecular, Cellular, and Developmental Biology and
2 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
3 Fungal Genomics Laboratory, North Carolina State University, Campus Box 7251, Raleigh, NC 27695-7251, USA.
4 Department of Anesthesiology, Yale University, New Haven, CT 06520, USA.
*   To whom correspondence should be addressed. E-mail: michael.snyder{at}yale.edu

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