Chemical-genomic dissection of the CTD code
JR Tietjen, DW Zhang, JB Rodríguez-Molina… - Nature structural & …, 2010 - nature.com
Sequential modifications of the RNA polymerase II (Pol II) C-terminal domain (CTD)
coordinate the stage-specific association and release of cellular machines during …
coordinate the stage-specific association and release of cellular machines during …
Different phosphoisoforms of RNA polymerase II engage the Rtt103 termination factor in a structurally analogous manner
The carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II)
orchestrates dynamic recruitment of specific cellular machines during different stages of …
orchestrates dynamic recruitment of specific cellular machines during different stages of …
Updating the RNA polymerase CTD code: adding gene-specific layers
S Egloff, M Dienstbier, S Murphy - Trends in Genetics, 2012 - cell.com
The carboxyl-terminal domain (CTD) of RNA polymerase (pol) II comprises multiple tandem
repeats with the consensus sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 that can be …
repeats with the consensus sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 that can be …
A feed forward circuit comprising Spt6, Ctk1 and PAF regulates Pol II CTD phosphorylation and transcription elongation
R Dronamraju, BD Strahl - Nucleic acids research, 2013 - academic.oup.com
The C-terminal domain (CTD) of RNA polymerase II is sequentially modified for recruitment
of numerous accessory factors during transcription. One such factor is Spt6, which couples …
of numerous accessory factors during transcription. One such factor is Spt6, which couples …
Gene-specific RNA polymerase II phosphorylation and the CTD code
Phosphorylation of the RNA polymerase (Pol) II C-terminal domain (CTD) repeats (1-
YSPTSPS-7) is coupled to transcription and may act as a'code'that controls mRNA synthesis …
YSPTSPS-7) is coupled to transcription and may act as a'code'that controls mRNA synthesis …
Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination
The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) serves an
important role in coordinating stage-specific recruitment and release of cellular machines …
important role in coordinating stage-specific recruitment and release of cellular machines …
Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain
The carboxy-terminal domain (CTD) of the RNA polymerase II (Pol II) large subunit cycles
through phosphorylation states that correlate with progression through the transcription …
through phosphorylation states that correlate with progression through the transcription …
CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II
A Mayer, M Heidemann, M Lidschreiber, A Schreieck… - Science, 2012 - science.org
In different phases of the transcription cycle, RNA polymerase (Pol) II recruits various factors
via its C-terminal domain (CTD), which consists of conserved heptapeptide repeats with the …
via its C-terminal domain (CTD), which consists of conserved heptapeptide repeats with the …
RNA polymerase II transcription elongation and Pol II CTD Ser2 phosphorylation: a tail of two kinases
EA Bowman, WG Kelly - Nucleus, 2014 - Taylor & Francis
The transition between initiation and productive elongation during RNA Polymerase II (Pol II)
transcription is a well-appreciated point of regulation across many eukaryotes. Elongating …
transcription is a well-appreciated point of regulation across many eukaryotes. Elongating …
Uniform transitions of the general RNA polymerase II transcription complex
A Mayer, M Lidschreiber, M Siebert, K Leike… - Nature structural & …, 2010 - nature.com
We present genome-wide occupancy profiles for RNA polymerase (Pol) II, its
phosphorylated forms and transcription factors in proliferating yeast. Pol II exchanges …
phosphorylated forms and transcription factors in proliferating yeast. Pol II exchanges …