RNA polymerase II C-terminal domain binding

Definition

Target type: molecularfunction

Binding to the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. The CTD is comprised of repeats of a heptapeptide with the consensus sequence YSPTSPS. The number of repeats varies with the species and a minimum number of repeats is required for RNAP II function. [PMID:20889714]

RNA polymerase II (RNAP II) C-terminal domain (CTD) binding is a crucial molecular interaction that plays a central role in the regulation of gene expression. The CTD is a highly conserved, repetitive domain located at the carboxyl terminus of the largest subunit of RNAP II. It consists of a heptapeptide repeat (YSPTSPS) that can be phosphorylated at multiple serine residues. These phosphorylation events, orchestrated by various kinases and phosphatases, create a dynamic code that governs the recruitment of different factors involved in transcription and RNA processing.

RNAP II CTD binding proteins recognize specific phosphorylation patterns on the CTD, allowing them to associate with RNAP II at specific stages of the transcription cycle. This interaction enables the coordinated recruitment of factors involved in:

- **Initiation:** CTD binding proteins such as TFIIF and mediator complex facilitate the initiation of transcription by recruiting RNAP II to promoters and interacting with general transcription factors.

- **Elongation:** As RNAP II transcribes DNA, the CTD becomes phosphorylated, creating binding sites for factors involved in elongation, such as capping enzymes and splicing factors.

- **Termination:** CTD phosphorylation patterns change during termination, signaling the detachment of RNAP II from the DNA template and the recruitment of factors responsible for mRNA 3' end processing.

- **RNA processing:** CTD binding proteins, including capping enzymes, splicing factors, and polyadenylation factors, bind to the phosphorylated CTD and carry out essential RNA processing events.

- **Chromatin modification:** CTD binding proteins can also interact with chromatin remodeling complexes, influencing chromatin structure and accessibility to RNAP II.

This intricate interplay between the CTD phosphorylation state and CTD binding proteins ensures the proper coordination of transcription and RNA processing, ultimately enabling the production of functional RNA molecules.'
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Proteins (1)

Compounds (45)