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

Research output: Contribution to journal › Journal article › peer-review

Standard

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

In: Journal of Biological Chemistry, Vol. 288, No. 21, 2013, p. 15110-15120.

Research output: Contribution to journal › Journal article › peer-review

Harvard

Taylor, NMI, Glatt, S, Hennrich, ML, von Scheven, G, Grötsch, H, Fernández-Tornero, C, Rybin, V, Gavin, A-C, Kolb, P & Müller, CW 2013, 'Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC', Journal of Biological Chemistry, vol. 288, no. 21, pp. 15110-15120. https://doi.org/10.1074/jbc.M112.427856

APA

Taylor, N. M. I., Glatt, S., Hennrich, M. L., von Scheven, G., Grötsch, H., Fernández-Tornero, C., Rybin, V., Gavin, A-C., Kolb, P., & Müller, C. W. (2013). Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. Journal of Biological Chemistry, 288(21), 15110-15120. https://doi.org/10.1074/jbc.M112.427856

Vancouver

Taylor NMI, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C et al. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. Journal of Biological Chemistry. 2013;288(21):15110-15120. https://doi.org/10.1074/jbc.M112.427856

Author

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. / Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 21. pp. 15110-15120.

Bibtex

@article{293b01e86e5441a2957bf5fd85365b74,
title = "Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC",
abstract = "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.",
keywords = "Crystallography, X-Ray, Molecular Docking Simulation, Phosphoric Monoester Hydrolases/chemistry, Protein Structure, Tertiary, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/chemistry, Transcription Factors, TFIII/chemistry",
author = "Taylor, {Nicholas M I} and Sebastian Glatt and Hennrich, {Marco L} and {von Scheven}, Gudrun and Helga Gr{\"o}tsch and Carlos Fern{\'a}ndez-Tornero and Vladimir Rybin and Anne-Claude Gavin and Peter Kolb and M{\"u}ller, {Christoph W}",
year = "2013",
doi = "10.1074/jbc.M112.427856",
language = "English",
volume = "288",
pages = "15110--15120",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "21",

}

RIS

TY - JOUR

T1 - Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC

AU - Taylor, Nicholas M I

AU - Glatt, Sebastian

AU - Hennrich, Marco L

AU - von Scheven, Gudrun

AU - Grötsch, Helga

AU - Fernández-Tornero, Carlos

AU - Rybin, Vladimir

AU - Gavin, Anne-Claude

AU - Kolb, Peter

AU - Müller, Christoph W

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Crystallography, X-Ray

KW - Molecular Docking Simulation

KW - Phosphoric Monoester Hydrolases/chemistry

KW - Protein Structure, Tertiary

KW - Saccharomyces cerevisiae/enzymology

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Transcription Factors, TFIII/chemistry

U2 - 10.1074/jbc.M112.427856

DO - 10.1074/jbc.M112.427856

M3 - Journal article

C2 - 23569204

VL - 288

SP - 15110

EP - 15120

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 21

ER -

ID: 194521274