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J. Biol. Chem., Vol. 276, Issue 33, 30956-30963, August 17, 2001
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§,
From the ¶ Department of Internal Medicine, University of
Texas Southwestern Medical Center, Dallas, Texas 75390-8573 and
An in vivo protein interaction assay
was used to search a yeast cDNA library for proteins that bind to
the acidic activation domain (AD) of the yeast Gal4 protein. Sug2
protein, a component of the 19 S regulatory particle of the 26 S
proteasome, was one of seven proteins identified in this screen.
In vitro binding assays confirm a direct interaction
between these proteins. SUG2 and SUG1, another
19 S component, were originally discovered as a mutation able to
suppress the phenotype of a Gal4 truncation mutant (Gal4Dp)
lacking much of its AD. Sug1p has previously been shown to bind the
Gal4 AD in vitro. Taken together, these genetic and
biochemical data suggest a biologically significant interaction between
the Gal4 protein and the 19 S regulatory particle of the proteasome. Indeed, it is demonstrated here that the Gal4 AD interacts specifically with immunopurified 19 S complex. The proteasome regulatory particle has been shown recently to play a direct role in RNA polymerase II
transcription and the activator-19 S interaction could be important in
recruiting this large complex to transcriptionally active
GAL genes.
Stratagene, Inc., La Jolla, California 92037
To whom correspondence should be addressed: Dept. of Internal
Medicine, University of Texas Southwestern Medical Center, 5323 Harry
Hines Blvd., Dallas, TX 75390-8573. Tel.: 214-648-1239; Fax:
214-648-1450; E-mail: thomas.kodadek@utsouthwestern.edu.
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