Yeast Genetics and Molecular Biology 2002
University of Wisconsin
Madison, Wisconsin USA
July 30 - August 4, 2002


Name: Miller, John P.
Mailing Address: Genome Sciences, University of Washington, 1959 NE Pacific St., Seattle, WA 98195-7730, United States of America
Email Address: jpm@u.washington.edu
Phone & FAX numbers: 12066164523 & 12066163690
URL: http://depts.washington.edu/sfields/

Abstract #36


Session Title: Proteomics
Session Time: Thursday, August 1 -- 4:30PM - 6:00PM
Presentation: Platform
Topic: Global Analysis

Identification of protein-protein interactions between integral membrane proteins.
John P. Miller (1), Safia Thaminy (2), Igor Stagljar (3), Stanley Fields (4)
(1) Genome Sciences, University of Washington, 1959 NE Pacific St., Seattle, WA 98195-7730, United States of America; (2) Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich-Irchel, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland; (3) Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich-Irchel and Dualsystems Biotech, Inc., Winterthurerstrasse 190, CH-8057 Zurich, Switzerland; (4) Howard Hughes Medical Institute, Department of Genome Sciences and Department of Medicine, University of Washington, Seattle, WA 98195-7730

We have generated an assay system to analyze interactions between integral membrane proteins in the hope that such information can provide clues as to the functions of these proteins. To this end, we created an array of yeast colonies each expressing a different integral membrane protein-fusion competent for use in the split-ubiquitin system originally developed by Johnsson and Varshavsky (PNAS 91:10340-10344 (1994)). The system is based on the ability of interacting proteins to bring two fragments of ubiquitin into close proximity such that they are acted on by ubiquitin-specific proteases. Proteolysis releases a reporter protein, in our case a transcription factor that then enters the nucleus to activate reporter genes (Stagljar et al. PNAS 95:5187-5192 (1998)). We selected proteins annotated in the Yeast Proteome Database as 'integral membrane' to place into the array. For each of the ~700 proteins in the array we generated constructs designed to make hybrids in two forms: with the membrane protein amino-terminal or carboxyl-terminal to one of the halves of ubiquitin. In a pilot project, we screened an array of ~40 membrane proteins against components of the OST complex, ER-associated degradation pathway, and translocation machinery, and we are planning to further study these and other membrane complexes against the larger array.


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