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Review
. 2013 Nov 13;113(11):8423-55.
doi: 10.1021/cr400158h. Epub 2013 Sep 16.

RNA polymerase II C-terminal domain: Tethering transcription to transcript and template

Jeffry L Corden  1
Affiliations
Review

RNA polymerase II C-terminal domain: Tethering transcription to transcript and template

Jeffry L Corden. Chem Rev. .
No abstract available

PubMed Disclaimer

Conflict of interest statement

The author declares no competing financial interest

Figures

Figure 1
Figure 1
Diagram showing the three regions of the CTD.
Figure 2
Figure 2
Idealized SDS PAGE separation of the Rpb1 subunit. Increasing phosphatase treatment increases the mobility of the IIo form while proteolysis increases the mobility of both forms. x refers to intermediate phosphorylation states while y refers to intermediates in CTD degradation.
Figure 3
Figure 3
Sequences of CTDs from different organisms. The sequences are aligned to emphasize the heptad repeat. Residues in red deviate from the consensus.
Figure 4
Figure 4
Phenotypes of CTD substitution mutants. Indicated phenotypes are due to substitution in each repeat. Red indicates lethal mutations while blue indicates viable mutations. Some mutations are listed as both viable and inviable depending one the organism as designated in subscripts (c = S. cerevisiae, p = S. pombe, and h = human).
Figure 5
Figure 5
Diagram showing the recognition of adjacent heptad repeats by the C. albicans capping enzyme CDS1 and CDS2 binding pockets. The dotted line indicates the potential position of additional repeats if the CDS1 and CDS2 binding pockets recognize heptads that are not adjacent but separated by one or more heptad repeat.
Figure 6
Figure 6
The CTD-interacting domain (CID). (a) Structures of the CID of Pcf11, Nrd1 and Scaf8 bound to CTD peptides. (b) Diagram showing the interaction of CID side chains with CTD residues. Black arrows indicate interactions with the ß-turn and preceding Tyr residue. Blue arrows indicate Scaf8 interactions with the downstream Tyr residue. Red arrows indicate interactions with phosphorylated Ser residues by Nrd1 and Scaf8. The position of these interactions is indicated by the same colors in part A. The wavey bond in the CTD peptide bound to Nrd1 indicates the cis conformation of this paptide bond. (c) Dotted lines indicate alternative binding modes for Pcf11 bound to a doubly phosphorylated CTD peptide. The solid line represents the interaction of SCAF8 with a doubly phosphorylated CTD repeat.
See this image and copyright information in PMC

References

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