Modulation of RNA polymerase II subunit composition by ubiquitylation

Emerging evidence suggests that components of the ubiquitin-proteasome system are involved in the regulation of gene expression. A variety of factors, including transcriptional activators, coactivators, and histones, are controlled by ubiquitylation, but the mechanisms through which this modificatio...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-12, Vol.105 (50), p.19649-19654
Main Authors: Daulny, Anne, Geng, Fuqiang, Muratani, Masafumi, Geisinger, Jonathan M, Salghetti, Simone E, Tansey, William P
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - metabolism
Antibodies
Biochemistry
Biological Sciences
Chromatin
Data processing
DNA-directed RNA polymerase
Enzymes
Gene expression
Gene Expression Regulation, Fungal
Histones
Mass spectroscopy
Molecular Sequence Data
Phosphorylation
Proteases
proteasomes
Protein structure
Protein Subunits - metabolism
Proteins
Proteomics
Ribonucleic acid
RNA
RNA polymerase
RNA Polymerase II - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins - metabolism
Subunit structure
Transcription
Transcription factors
Transcriptional regulatory elements
Ubiquitin
Ubiquitin - genetics
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Ubiquitins
Yeast
Yeasts
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Summary:Emerging evidence suggests that components of the ubiquitin-proteasome system are involved in the regulation of gene expression. A variety of factors, including transcriptional activators, coactivators, and histones, are controlled by ubiquitylation, but the mechanisms through which this modification can function in transcription are generally unknown. Here, we report that the Saccharomyces cerevisiae protein Asr1 is a RING finger ubiquitin-ligase that binds directly to RNA polymerase II via the carboxyl-terminal domain (CTD) of the largest subunit of the enzyme. We show that interaction of Asr1 with the CTD depends on serine-5 phosphorylation within the CTD and results in ubiquitylation of at least 2 subunits of the enzyme, Rpb1 and Rpb2. Ubiquitylation by Asr1 leads to the ejection of the Rpb4/Rpb7 heterodimer from the polymerase complex and is associated with inactivation of polymerase function. Our data demonstrate that ubiquitylation can directly alter the subunit composition of a core component of the transcriptional machinery and provide a paradigm for how ubiquitin can influence gene activity.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0809372105