Phosphorylation and functions of the RNA polymerase II CTD.
By Hemali P. Phatnani, A. Greenleaf. Genes & Development, 2006
811 citations recorded by the source corpus.
The C-terminal repeat domain (CTD), an unusual extension appended to the C terminus of the largest subunit of RNA polymerase II, serves as a flexible binding scaffold for numerous nuclear factors; which factors bind is determined by the phosphorylation patterns on the CTD repeats. Changes in phosphorylation patterns, as polymerase transcribes a gene, are thought to orchestrate the association of different sets of factors with the transcriptase and strongly influence functional organization of the nucleus. In this review we appraise what is known, and what is not known, about patterns of phosphorylation on the CTD of RNA polymerases II at the beginning, the middle, and the end of genes; the proposal that doubly phosphorylated repeats are present on elongating polymerase is explored. We discuss briefly proteins known to associate with the phosphorylated CTD at the beginning and ends of genes; we explore in more detail proteins that are recruited to the body of genes, the diversity of their functions, and the potential consequences of tethering these functions to elongating RNA polymerase II. We also discuss accumulating structural information on phosphoCTD-binding proteins and how it illustrates the variety of binding domains and interaction modes, emphasizing the structural flexibility of the CTD. We end with a number of open questions that highlight the extent of what remains to be learned about the phosphorylation and functions of the CTD.
Subfields: Archeology
View Paper: https://www.semanticscholar.org/paper/412392272618f6fd4ecd438b9acfe8b5ad649be1
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In Archeology
Citations in the corpus
- Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches (2009, background): “The carboxy-terminal domain of the largest subunit of RNAP II consists of up to 52 tandem repeats of the heptapeptide consensus sequence YSPTSP”
- Structural insights to how mammalian capping enzyme reads the CTD code (2011, neutral): “The CTD is essential, and it serves as a landing platform for factors that regulate and/or catalyze mRNA processing and gene expression (Buratowski, 2009; Phatnani and Greenleaf, 2006).”
- Understanding the language of Lys36 methylation at histone H3 (2012, neutral): “This interaction is regulated by phosphorylated residues in the CTD of Rbp1, the large subunit of RNAPII: the Ser2-phosphorylated form of the CTD is indicative of elongation and the Ser5-phosphorylated form is characteristic of a paused polymerase at a promote”
- Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells (2007, neutral): “dtd" [ ]> Changes in phosphorylation of the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP) are associated with transcription initiation, elongation and terminatio”
- Preferential associations between co-regulated genes reveal a transcriptional interactome in erythroid cells (2009, neutral): “First, to focus on gene interactions within transcription factories, we included a ChIP step with an antibody recognizing the phosphorylated Ser5 residue of the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (RNAPII-S5P), the form implicated in transcriptional initiation and elo”
- Transcription Factors Bind Thousands of Active and Inactive Regions in the Drosophila Blastoderm (2008, background): “antibody recognizing the phosphorylated form of the Cterminal heptapeptide repeat of RNA polymerase II [27].”
- CDK8/9 drive Smad transcriptional action, turnover and YAP interactions in BMP and TGFβ pathways (2009, positive): “CDK8 and CDK9 phosphorylate overlapping serine clusters in the C-terminal domain of RNAP II (Phatnani and Greenleaf, 2006), a region which integrates regulatory inputs by binding proteins involved in mRNA biogenesis (Phatnani and Greenleaf, 2006).”
- An ATM-Dependent Transcriptional Silencing Program is Transmitted Through Chromatin in Cis to DNA Double Strand Breaks (2010, background): “Moreover, RNAPI is not subject to the regulatory CTD phosphorylations that are perturbed in DSB-induced RNAPII stalling (Phatnani and Greenleaf, 2006).”