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The carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II comprises multiple tandem conserved heptapeptide repeats, unique to this eukaryotic RNA polymerase. This unusual structure provides a docking platform for factors involved in various co-transcriptional events. Recruitment of the appropriate factors at different stages of the transcription cycle is achieved through changing patterns of post-translational modification of the CTD repeats, which create a readable 'code'. A new phosphorylation mark both expands the CTD code and provides the first example of a CTD signal read in a gene type-specific manner. How and when is the code written and read? How does it contribute to transcription and coordinate RNA processing?

Original publication




Journal article


Trends Genet

Publication Date





280 - 288


Amino Acid Motifs, Amino Acid Sequence, Animals, Endoribonucleases, Histone Code, Humans, Models, Biological, Peptide Elongation Factors, Protein Binding, Protein Processing, Post-Translational, Protein Structure, Tertiary, RNA Polymerase II, Transcription, Genetic