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

Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C, Rybin V, Gavin AC, Kolb P, Müller CW
J Biol Chem 288 15110-20 (2013)
Cited: 8 times
EuropePMC logo PMID: 23569204

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.

Articles - 2yn2 mentioned but not cited (1)

  1. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C, Rybin V, Gavin AC, Kolb P, Müller CW. J Biol Chem 288 15110-15120 (2013)


Reviews citing this publication (1)

  1. RNA polymerase I and III: similar yet unique. Khatter H, Vorländer MK, Müller CW. Curr Opin Struct Biol 47 88-94 (2017)

Articles citing this publication (6)

  1. Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. Male G, von Appen A, Glatt S, Taylor NM, Cristovao M, Groetsch H, Beck M, Müller CW. Nat Commun 6 7387 (2015)
  2. RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74. Taylor NM, Baudin F, von Scheven G, Müller CW. Nucleic Acids Res 41 9183-9196 (2013)
  3. Function of TFIIIC, RNA polymerase III initiation factor, in activation and repression of tRNA gene transcription. Ciesla M, Skowronek E, Boguta M. Nucleic Acids Res 46 9444-9455 (2018)
  4. Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation. Vorländer MK, Jungblut A, Karius K, Baudin F, Grötsch H, Kosinski J, Müller CW. Nat Commun 11 4905 (2020)
  5. Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation. Talyzina A, Han Y, Banerjee C, Fishbain S, Reyes A, Vafabakhsh R, He Y. Mol Cell 83 2641-2652.e7 (2023)
  6. Characterization of Tau95 led to the identification of a four-subunit TFIIIC complex in trypanosomatid parasites. Mondragón-Rosas F, Florencio-Martínez LE, Villa-Delavequia GS, Manning-Cela RG, Carrero JC, Nepomuceno-Mejía T, Martínez-Calvillo S. Appl Microbiol Biotechnol 108 109 (2024)


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