Updating the rna polymerase ctd code

28-Apr-2016 20:00

Dynamic phosphorylation of Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 heptad-repeats in the C-terminal domain (CTD) of the large subunit coordinates progression of RNA polymerase (Pol) II through the transcription cycle.

Here, we describe an M phase-specific form of Pol II phosphorylated at Thr4, but not at Tyr1, Ser2, Ser5, and Ser7 residues.

Thr4 phosphorylated Pol II binds to centrosomes and midbody and interacts with the Thr4-specific Polo-like kinase 1.

Binding of Pol II to centrosomes does not require the CTD but may involve subunits of the non-canonical R2TP-Prefoldin-like complex, which bind to and co-localize with Pol II at centrosomes.

Whereas the CTD docking sites are dominated in each case by interactions of the NTase domain with Ser5-POP).

Finally, we bring into focus new results that identify two additional CTD-associated processes: nucleocytoplasmic transport of m RNA and DNA damage and repair.

Since its discovery by Fischer and Krebs in 1955 [1], the reversible phosphorylation of proteins has been implicated in the regulation of almost every aspect of cellular function, including metabolism, cell division, differentiation, signaling, and countless others.

These phosphorylation events stimulate m RNA processing, however, it is not clear whether splicing activity affects the phosphorylation status of Pol II.

In this study, we found that splicing inhibition by potent splicing inhibitors spliceostatin A (SSA) and pladienolide B or by antisense oligos against sn RNAs decreased phospho-Ser2 level, but had little or no effects on phospho-Ser5 level.

Whereas the CTD docking sites are dominated in each case by interactions of the NTase domain with Ser5-POP).Finally, we bring into focus new results that identify two additional CTD-associated processes: nucleocytoplasmic transport of m RNA and DNA damage and repair.Since its discovery by Fischer and Krebs in 1955 [1], the reversible phosphorylation of proteins has been implicated in the regulation of almost every aspect of cellular function, including metabolism, cell division, differentiation, signaling, and countless others.These phosphorylation events stimulate m RNA processing, however, it is not clear whether splicing activity affects the phosphorylation status of Pol II.In this study, we found that splicing inhibition by potent splicing inhibitors spliceostatin A (SSA) and pladienolide B or by antisense oligos against sn RNAs decreased phospho-Ser2 level, but had little or no effects on phospho-Ser5 level.A particularly fascinating form of this regulation is employed during the transcription of DNA by RNA Polymerase II (RNAPII).