Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC
Research output: Contribution to journal › Journal article › peer-review
Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal histidine phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. We solved the crystal structures of τ55-HPD and its closely related paralogue Huf and used in silico docking methods to identify phosphoserine- and phosphotyrosine-containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. A comparative phosphoproteomic study identified additional phosphopeptides as possible targets that show the involvement of these two phosphatases in the regulation of a variety of cellular functions. Our results identify τ55-HPD and Huf as bona fide protein phosphatases, characterize their substrate specificities, and provide a small set of regulated phosphosite targets in vivo.
|Journal||Journal of Biological Chemistry|
|Number of pages||11|
|Publication status||Published - 2013|
- Crystallography, X-Ray, Molecular Docking Simulation, Phosphoric Monoester Hydrolases/chemistry, Protein Structure, Tertiary, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/chemistry, Transcription Factors, TFIII/chemistry