Recruitment of a 19 S Proteasome Subcomplex to an Activated Promoter
- 19 April 2002
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 296 (5567), 548-550
- https://doi.org/10.1126/science.1069490
Abstract
The 19 S proteasome regulatory particle plays a critical role in cellular proteolysis. However, recent reports have demonstrated that 19 S proteins play a nonproteolytic role in nucleotide excision repair and transcription elongation. We show by chromatin immunoprecipitation assays that proteins comprising the 19 S complex are recruited to the GAL1-10 promoter by the Gal4 transactivator upon induction with galactose. This recruited complex does not contain proteins from the 20 S proteolytic particle and includes a subset of the 19 S proteins. This subset is also specifically retained from an extract by the Gal4 activation domain. These data indicate that in vivo, the base of the 19 S complex functions independently of the larger complex and plays a direct, nonproteolytic role in RNA polymerase II transcription.Keywords
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