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Mediator Phosphorylation Prevents Stress Response Transcription During Non-stress Conditions

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78370

Matic,  Ivan
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78356

Mann,  Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Miller, C., Matic, I., Maier, K. C., Schwalb, B., Roether, S., Straesser, K., et al. (2012). Mediator Phosphorylation Prevents Stress Response Transcription During Non-stress Conditions. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(53), 44017-44026. doi:10.1074/jbc.M112.430140.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000E-8B8D-1
Abstract
The multiprotein complex Mediator is a coactivator of RNA polymerase (Pol) II transcription that is required for the regulated expression of protein-coding genes. Mediator serves as an end point of signaling pathways and regulates Pol II transcription, but the mechanisms it uses are not well understood. Here, we used mass spectrometry and dynamic transcriptome analysis to investigate a functional role of Mediator phosphorylation in gene expression. Affinity purification and mass spectrometry revealed that Mediator from the yeast Saccharomyces cerevisiae is phosphorylated at multiple sites of 17 of its 25 subunits. Mediator phosphorylation levels change upon an external stimulus set by exposure of cells to high salt concentrations. Phosphorylated sites in the Mediator tail subunit Med15 are required for suppression of stress-induced changes in gene expression under non-stress conditions. Thus dynamic and differential Mediator phosphorylation contributes to gene regulation in eukaryotic cells.