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Título

Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC

Autor Taylor, Nicholas M. I.; Glatt, Sebastian; Hennrich, Marco L.; von Scheven, Gudrun; Grötsch, Helga; Fernández-Tornero, Carlos ; Rybin, Vladimir; Gavin, Anne-Claude; Kolb, Peter; Müller, Christoph W.
Palabras clave Enzyme structure
Histidine phosphatase family
Mass spectrometry (MS)
Metabolism
Molecular docking
Phosphoproteomics
Protein phosphatase
RNA polymerase III
Transcription regulation
X-ray crystallography
Fecha de publicación 24-may-2013
EditorAmerican Society for Biochemistry and Molecular Biology
Citación J Biol Chem. 288(21):15110-20 (2013)
ResumenSaccharomyces 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.
Descripción 12 p.-5 fig.-2 tab.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M112.427856
URI http://hdl.handle.net/10261/155086
DOI10.1074/jbc.M112.427856
ISSN0021-9258
E-ISSN1083-351X
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