ArticleMolecular cell2013
The C-terminal domain of Rpb1 functions on other RNA polymerase II subunits.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
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- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- A mitogen-activated protein kinase PoxMK1 mediates regulation of the production of plant-biomass-degrading enzymes, vegetative growth, and pigment biosynthesis in Penicillium oxalicum.Applied microbiology and biotechnology · 2021Article
- Yeast Spt6 Reads Multiple Phosphorylation Patterns of RNA Polymerase II C-Terminal Domain In Vitro.Journal of molecular biology · 2020Article
- The Roles of Cyclin-Dependent Kinases in Cell-Cycle Progression and Therapeutic Strategies in Human Breast Cancer.International journal of molecular sciences · 2020Review
- A SUMO-dependent pathway controls elongating RNA Polymerase II upon UV-induced damage.Scientific reports · 2019Article
- MIR sequences recruit zinc finger protein ZNF768 to expressed genes.Nucleic acids research · 2019Article
- Determinants of Histone H3K4 Methylation Patterns.Molecular cell · 2017Article
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- Distributive O-GlcNAcylation on the Highly Repetitive C-Terminal Domain of RNA Polymerase II.Biochemistry · 2016Article
- Direct Analysis of Phosphorylation Sites on the Rpb1 C-Terminal Domain of RNA Polymerase II.Molecular cell · 2016Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- The evolutionarily conserved Pol II flap loop contributes to proper transcription termination on short yeast genes.Cell reports · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The C-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II (RNApII), coordinates recruitment of RNA- and chromatin-modifying factors to transcription complexes. It is unclear whether the CTD communicates with the catalytic core region of Rpb1 and thus must be physically connected, or instead can function as an independent domain. To address this question, CTD was transferred to other RNApII subunits. Fusions to Rpb4 or Rpb6, two RNApII subunits located near the original position of CTD, support viability in a strain carrying a truncated Rpb1. In contrast, CTD fusion to Rpb9 on the other side of RNApII does not. Rpb4-CTD and Rpb6-CTD proteins are functional for phosphorylation and recruitment of various factors, albeit with some restrictions and minor defects. Normal CTD functions are not transferred to RNApI or RNApIII by Rbp6-CTD. These results show that, with some spatial constraints, CTD can function even when disconnected from Rpb1.
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