ArticleThe Journal of biological chemistry2013
Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural and kinetic insights into tRNA promoter engagement by yeast general transcription factor TFIIIC.Nucleic acids research · 2025Article
- Characterization of Tau95 led to the identification of a four-subunit TFIIIC complex in trypanosomatid parasites.Applied microbiology and biotechnology · 2024Article
- Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation.Molecular cell · 2023Article
- Structural insights into human TFIIIC promoter recognition.Science advances · 2023Article
- Structural basis of TFIIIC-dependent RNA Polymerase III transcription initiation.bioRxiv : the preprint server for biology · 2023Article
- Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation.Nature communications · 2020Article
- Function of TFIIIC, RNA polymerase III initiation factor, in activation and repression of tRNA gene transcription.Nucleic acids research · 2018Article
- Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.Nature communications · 2015Article
- Solving the RNA polymerase I structural puzzle.Acta crystallographica. Section D, Biological crystallography · 2014Article
- RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74.Nucleic acids research · 2013Article
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Authors and funding
10 authors.
Funding
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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.
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