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Review
. 2002 Apr;1(2):153-62.
doi: 10.1128/EC.1.2.153-162.2002.

RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function

Gregory Prelich  1
Affiliations
Review

RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function

Gregory Prelich. Eukaryot Cell. 2002 Apr.
No abstract available

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Figures

FIG. 1.
FIG. 1.
A working model for sequential activities of the CTD kinases. CTD phosphorylation varies during the transcription cycle, driven by multiple CTD kinases. A working model for their sequential activities is depicted here, based on results summarized in the text. Unphosphorylated pol II is preferentially recruited to the promoter, driven by interactions with initiation factors such as TBP and the mediator complex. Shortly after initiation, the CTD is phosphorylated on serine 5 by Kin28/Cdk7, stimulating promoter escape and binding of the Ceg1 subunit of capping enzyme. Productive elongation is stimulated by P-TEFb, Ctk1, and Bur1, resulting in a shift to a form containing phosphorylated serine 2. CTD phosphorylation stimulates binding of several splicing, elongation, and 3′ end processing factors, but the responsible kinases and their order of recruitment are not clear. Subsequent dephosphorylation by the Fcp1 phosphatase allows recycling of pol II into a reinitiation-competent form. Phosphorylation of free pol II by Srb10/Cdk8 on serine 5 is proposed to block initiation.
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