Physical and Functional Association of RNA Polymerase II and the Proteasome

Recent studies from a number of laboratories have revealed a surprising number of connections between RNA polymerase II transcription and the ubiquitin/proteasome pathway. We now find yet another intersection of these pathways by showing that the 26S proteasome associates with regions of the GAL1, G...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 101; no. 16; pp. 5904 - 5909
Main Authors Gillette, Thomas G., Gonzalez, Fernando, Delahodde, Agnes, Johnston, Stephen Albert, Kodadek, Thomas, Varshavsky, Alexander
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 20.04.2004
National Acad Sciences
Subjects
Antibodies
Biochemistry
Biological Sciences
Cysteine Endopeptidases - metabolism
Cysteine Endopeptidases - physiology
DNA
Gene induction
Genes
Hydrolysis
Multienzyme Complexes - metabolism
Multienzyme Complexes - physiology
Polymerase chain reaction
Precipitin Tests
Promoter regions
Proteasome Endopeptidase Complex
Ribonucleic acid
RNA
RNA Polymerase II - metabolism
RNA Polymerase II - physiology
Shock heating
Terminator regions
Transcription, Genetic
Yeasts
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Summary:Recent studies from a number of laboratories have revealed a surprising number of connections between RNA polymerase II transcription and the ubiquitin/proteasome pathway. We now find yet another intersection of these pathways by showing that the 26S proteasome associates with regions of the GAL1, GAL10, and HSP82 genes, including the 3′ ends, in a transcription-dependent fashion. The appearance of the proteasome on these inducible genes correlates with both the accumulation of transcripts and the buildup of RNA polymerase II complexes in the same region. Furthermore, the 26S proteasome and RNA polymerase II coimmunoprecipitate, and inhibition of 26S proteolytic activity leads to increased read through of a transcription termination site. We suggest that the proteasome is generally recruited to the DNA at sites of stalled RNA polymerase and may act to resolve these complexes.
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This paper was submitted directly (Track II) to the PNAS office.
Edited by Alexander Varshavsky, California Institute of Technology, Pasadena, CA, and approved February 20, 2004
To whom correspondence should be addressed. E-mail: stephen.johnston@utsouthwestern.edu or thomas.kodadek@utsouthwestern.edu.
Abbreviations: ChIP, chromatin immunoprecipitation; pol II, polymerase II; β-gal, β-galactosidase.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0305411101