Global Analysis of Protein Activities Using Proteome Chips
- Heng Zhu1,
- Metin Bilgin1,
- Rhonda Bangham1,
- David Hall2,
- Antonio Casamayor1,
- Paul Bertone1,
- Ning Lan2,
- Ronald Jansen2,
- Scott Bidlingmaier2,
- Thomas Houfek3,
- Tom Mitchell3,
- Perry Miller4,
- Ralph A. Dean3,
- Mark Gerstein2,
- Michael Snyder1,2,*
- 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 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.
↵* To whom correspondence should be addressed. E-mail:
- Received for publication 2 May 2001.
- Accepted for publication 13 July 2001.