scholarly journals Arginine Citrullination at the C-Terminal Domain Controls RNA Polymerase II Transcription

2019 ◽  
Vol 73 (1) ◽  
pp. 84-96.e7 ◽  
Author(s):  
Priyanka Sharma ◽  
Antonios Lioutas ◽  
Narcis Fernandez-Fuentes ◽  
Javier Quilez ◽  
José Carbonell-Caballero ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Terminal Domain ◽  
Rna Polymerase Ii Transcription

Role of C-terminal domain phosphorylation in RNA polymerase II transcription through the nucleosome

Biopolymers ◽  
2003 ◽  
Vol 68 (4) ◽  
pp. 528-538 ◽  
Author(s):  
Y. V. Liu ◽  
D. J. Clark ◽  
V. Tchernajenko ◽  
M. E. Dahmus ◽  
V. M. Studitsky
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Terminal Domain ◽  
Rna Polymerase Ii Transcription

scholarly journals CDK12 globally stimulates RNA polymerase II transcription elongation and carboxyl-terminal domain phosphorylation

2020 ◽  
Vol 48 (14) ◽  
pp. 7712-7727
Author(s):  
Michael Tellier ◽  
Justyna Zaborowska ◽  
Livia Caizzi ◽  
Eusra Mohammad ◽  
Taras Velychko ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Elongation ◽  
Pol Ii ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Genome Wide ◽  
A Genome ◽  
Carboxyl Terminal ◽  
Rna Polymerase Ii Transcription

Abstract Cyclin-dependent kinase 12 (CDK12) phosphorylates the carboxyl-terminal domain (CTD) of RNA polymerase II (pol II) but its roles in transcription beyond the expression of DNA damage response genes remain unclear. Here, we have used TT-seq and mNET-seq to monitor the direct effects of rapid CDK12 inhibition on transcription activity and CTD phosphorylation in human cells. CDK12 inhibition causes a genome-wide defect in transcription elongation and a global reduction of CTD Ser2 and Ser5 phosphorylation. The elongation defect is explained by the loss of the elongation factors LEO1 and CDC73, part of PAF1 complex, and SPT6 from the newly-elongating pol II. Our results indicate that CDK12 is a general activator of pol II transcription elongation and indicate that it targets both Ser2 and Ser5 residues of the pol II CTD.

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