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Recruitment of a 19S Proteasome Subcomplex to an Activated Promoter
Fernando Gonzalez,*Agnes Delahodde,*Thomas Kodadek,Stephen Albert Johnston
The 19S proteasome regulatory particle plays a critical
role in cellular proteolysis. However, recent reports have demonstratedthat 19S proteins play a nonproteolytic role in nucleotide
excisionrepair and transcription elongation. We show by chromatin
immunoprecipitationassays that proteins comprising the 19S
complex are recruitedto the GAL1-10 promoter by the Gal4
transactivator upon inductionwith galactose. This recruited complex
does not contain proteinsfrom the 20S proteolytic particle
and includes a subset of the19S proteins. This subset is
also specifically retained from anextract by the Gal4 activation
domain. These data indicate thatin vivo, the base of the
19S complex functions independently ofthe larger complex
and plays a direct, nonproteolytic role inRNA polymerase II
transcription.
Center for Biomedical Inventions, University of Texas-Southwestern
Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-8573,
USA.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
stephen.johnston{at}utsouthwestern.edu
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