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A more recent version of this article appeared on August 10, 2001
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M102254200v1
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Papers In Press, published online ahead of print June 19, 2001
J. Biol. Chem, 10.1074/jbc.M102254200
Submitted on March 13, 2001
Revised on June 13, 2001
Accepted on June 18, 2001

The Gal4 activation domain binds Sug2 protein, a proteasome component, In vivo and in vitro

Cathy Chang, Fernando Gonzalez, Beverly Rothermel, Liping Sun, Stephen Albert Johnston, and Thomas Kodadek

Internal Medicine and Biochemistry, UT-Southwestern Medical Center, Dallas, TX 75390-8573

Corresponding Author: thomas.kodadek{at}utsouthwestern.edu

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 19S regulatory particle of the 26S 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 19S 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 19S regulatory particle of the proteasome. Indeed, it is demonstrated here that the Gal4 AD interacts specifically with immunopurified 19S complex. The proteasome regulatory particle has recently been shown to play a direct role in RNA polymerase II transcription and the activator-19S interaction could be important in recruiting this large complex to transcriptionally active GAL genes.


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