ArticleACS chemical biology2013
novel modifications on C-terminal domain of RNA polymerase II can fine-tune the phosphatase activity of Ssu72.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 32 citations in OpenAlex.
- [Vacuum ultraviolet laser dissociation and proteomic analysis of halogenated peptides].Se pu = Chinese journal of chromatography · 2025Article
- Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription.Nature communications · 2024Article
- ThrScience advances · 2024Article
- Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription.bioRxiv : the preprint server for biology · 2024Article
- Simplicity is the Ultimate Sophistication-Crosstalk of Post-translational Modifications on the RNA Polymerase II.Journal of molecular biology · 2021Review
- Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases.International journal of molecular sciences · 2021Review
- Diverse and conserved roles of the protein Ssu72 in eukaryotes: from yeast to higher organisms.Current genetics · 2021Review
- Structural determinants for accurate dephosphorylation of RNA polymerase II by its cognate C-terminal domain (CTD) phosphatase during eukaryotic transcription.The Journal of biological chemistry · 2019Article
- Methods review: Mass spectrometry analysis of RNAPII complexes.Methods (San Diego, Calif.) · 2019Review
- Extensive Characterization of Heavily Modified Histone Tails by 193 nm Ultraviolet Photodissociation Mass Spectrometry via a Middle-Down Strategy.Analytical chemistry · 2018Article
- Chemical Tools for Studying the Impact of cis/trans Prolyl Isomerization on Signaling: A Case Study on RNA Polymerase II Phosphatase Activity and Specificity.Methods in enzymology · 2018Article
- Different phosphoisoforms of RNA polymerase II engage the Rtt103 termination factor in a structurally analogous manner.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.Nature communications · 2017Article
- Mapping the Phosphorylation Pattern of Drosophila melanogaster RNA Polymerase II Carboxyl-Terminal Domain Using Ultraviolet Photodissociation Mass Spectrometry.ACS chemical biology · 2017Article
- 193 nm Ultraviolet Photodissociation Mass Spectrometry for Phosphopeptide Characterization in the Positive and Negative Ion Modes.Journal of proteome research · 2016Article
- Dephosphorylating eukaryotic RNA polymerase II.Biochimica et biophysica acta · 2016Review
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2016Review
- Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.ACS chemical biology · 2015Article
- Improvement of shotgun proteomics in the negative mode by carbamylation of peptides and ultraviolet photodissociation mass spectrometry.Analytical chemistry · 2014Article
- Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Molecular and cellular biology · 2014Review
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7 authors at 1 institution in 1 country.
Funding
Abstract
The C-terminal domain of RNA polymerase II (CTD) modulates the process of transcription through sequential phosphorylation/dephosphorylation of its heptide repeats, through which it recruits various transcription regulators. Ssu72 is the first characterized cis-specific CTD phosphatase that dephosphorylates Ser5 with a requirement for the adjacent Pro6 in a cis conformation. The recent discovery of Thr4 phosphorylation in the CTD calls into question whether such a modification can interfere with Ssu72 binding via the elimination of a conserved intramolecular hydrogen bond in the CTD that is potentially essential for recognition. To test if Thr4 phosphorylation will abolish Ser5 dephosphorylation by Ssu72, we determined the kinetic and structural properties of Drosophila Ssu72-symplekin in complex with the CTD peptide with consecutive phosphorylated Thr4 and Ser5. Our mass spectrometric and kinetic data established that Ssu72 does not dephosphorylate Thr4, but the existence of phosphoryl-Thr4 next to Ser5 reduces the activity of Ssu72 toward the CTD peptide by 4-fold. To our surprise, even though the intramolecular hydrogen bond is eliminated due to the phosphorylation of Thr4, the CTD adopts an almost identical conformation to be recognized by Ssu72 with Ser5 phosphorylated alone or both Thr4/Ser5 phosphorylated. Our results indicate that Thr4 phosphorylation will not abolish the essential Ssu72 activity, which is needed for cell survival. Instead, the phosphatase activity of Ssu72 is fine-tuned by Thr4 phosphorylation and eventually may lead to changes in transcription. Overall, we report the first case of structural and kinetic effects of phosphorylated Thr4 on CTD modifying enzymes. Our results support a model in which a combinatorial cascade of CTD modification can modulate transcription.
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