Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain
The RNA polymerase II C-terminal domain acts as a hub to coordinate transcription and nascent mRNA processing. Here the authors identify a phosphorylation-dependent switch in thetrans-to-cisisomerization of proline in the CTD heptad repeats that make those repeats susceptible to further modification...
Main Authors: | Eric B. Gibbs, Feiyue Lu, Bede Portz, Michael J. Fisher, Brenda P. Medellin, Tatiana N. Laremore, Yan Jessie Zhang, David S. Gilmour, Scott A. Showalter |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2017-05-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms15233 |
Similar Items
-
Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain
by: Bede Portz, et al.
Published: (2017-05-01) -
The RNA polymerase II C-terminal domain : its phosphorylation and interaction with the mediator complex
by: Soegaard, Teit Max Moscote
Published: (2006) -
Phosphorylation Status of RNA Polymerase II Carboxyl-terminal Domain in Porcine Oocytes and Early Embryos
by: Reza K. Oqani, et al.
Published: (2012-06-01) -
Tyr1 phosphorylation promotes phosphorylation of Ser2 on the C-terminal domain of eukaryotic RNA polymerase II by P-TEFb
by: Joshua E Mayfield, et al.
Published: (2019-08-01) -
Abstract P-18: Phosphorylation of RNA Polymerase II C-Terminal Domain Affects Transcript Elongation Through Chromatin
by: Sohail Akhtar, et al.
Published: (2021-06-01)