Progression through the RNA polymerase II CTD cycle
By S. Buratowski. Molecules and Cells, 2009
810 citations recorded by the source corpus.
Summary The C-terminal domain of the RNA polymerase II largest subunit undergoes dynamic phosphorylation during transcription, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA processing and histone modifying factors. Recent papers help explain how the changes in CTD phosphorylation pattern are linked to the progression from initiation through elongation to termination.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b05ea06d5987f3e3d7bc3187ee964a845929ffa7
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In Molecular Biology
- Jing-Ping Hsin
- Stewart Shuman
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- Masahiko Imashimizu
Citations in the corpus
- Structural insights to how mammalian capping enzyme reads the CTD code (2011, positive): “Reading the CTD Code: Diversity in CTD Conformation and Recognition Despite being composed of a repeating heptapeptide sequence, the CTD is able to interact with a multitude of RNA processing factors in a coordinated fashion during various stages of transcription (Buratowski, 2009).”
- The RNA polymerase II CTD coordinates transcription and RNA processing. (2012, background): “…dimethylation and CTD Ser5-P are then involved in recruiting the Set3 complex, a histone deacetylase that deactylates histones H3 and H4, leading to reduced histone acetylation levels at the 59 ends of genes, which promotes the association of RNAP II (Kim and Buratowski 2009; Govind et al. 2010).”
- CTCF-promoted RNA polymerase II pausing links DNA methylation to splicing (2011, positive): “Using antibodies specific to pol II phosphorylated on the carboxy-terminal domain (CTD), we further showed that elevated pol II at CD45 exon 5 in RB high cells is associated with the elongating form phosphorylated on serine 2 of CTD YSPTSPS heptad repeat”