Global Analysis of Protein Activities Using Proteome Chips

Author:

Zhu Heng1,Bilgin Metin1,Bangham Rhonda1,Hall David2,Casamayor Antonio1,Bertone Paul1,Lan Ning2,Jansen Ronald2,Bidlingmaier Scott2,Houfek Thomas3,Mitchell Tom3,Miller Perry4,Dean Ralph A.3,Gerstein Mark2,Snyder Michael12

Affiliation:

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.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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