Global analysis of protein activities using proteome chips.

Zhu H, Bilgin M, Bangham R, Hall D, Casamayor A, Bertone P, Lan N, Jansen R, Bidlingmaier S, Houfek T, Mitchell T, Miller P, Dean RA, Gerstein M, Snyder M
Science. 2001 293 (5537): 2101-5

PMID: 11474067 · DOI:10.1126/science.1062191

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.

MeSH Terms (22)

Amino Acid Motifs Amino Acid Sequence Calmodulin Calmodulin-Binding Proteins Cell Membrane Cloning, Molecular Fungal Proteins Glucose Liposomes Membrane Proteins Molecular Sequence Data Open Reading Frames Peptide Library Phosphatidylcholines Phosphatidylinositols Phospholipids Protein Binding Proteome Recombinant Fusion Proteins Saccharomyces cerevisiae Signal Transduction Streptavidin

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