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Physiol. Genomics 7: 27-34, 2001;
1094-8341/01 $5.00
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Received 14 March 2001; accepted in final form 1 August 2001.
Physiological Genomics 7:27-34 (2001)
1094-8341/01 $5.00 © 2001 American Physiological Society

Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome

GERARD CAGNEY1, PETER UETZ1 and STANLEY FIELDS1,2

1 Departments of Genetics and Medicine
2 Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195-7360

A two-hybrid screen against an activation domain array of Saccharomyces cerevisiae proteins was carried out for 31 yeast proteasome proteins. Fifty-five putative interactions were identified: 21 between components of the proteasome complex and 34 between proteasome proteins and other proteins. Many of these latter interactions involved either proteins of the ubiquitin pathway, cell cycle proteins, protein kinases or a translation initiation factor subunit. The role of eleven proteins associated with proteasome function by these screens was analyzed by examining the corresponding deletion strains for temperature sensitivity and canavanine sensitivity and for the stability of a ubiquitin-ß-galactosidase fusion protein. These assays additionally implicated three proteins, Bim1, Ump1, and YKL171W, in proteasome function. This study demonstrates the utility of genome-wide two-hybrid assays as an entry point for the further analysis of a large protein complex.

protein degradation; protein interactions; ubiquitin




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