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Special Flood Hazard Area inundated by the 100-year flood; with flood depths of 1 to 3 feet (usually sheet flow on the sloping terrain); average depths are determined.
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The eukaryotic RNA polymerase II (RNAPII) catalyzes the transcription of all protein encoding genes and is also responsible for the generation of small regulatory RNAs.
RNAPII has evolved a unique domain composed of heptapeptide repeats with the consensus sequence Tyr1–Ser2–Pro3–Thr4–Ser5–Pro6–Ser7 at the C-terminus (CTD) of its largest subunit (Rpb1).
The capping reactions are universal in eukarya and the formation of guanylate caps is essential in all species that have been examined genetically.
We have shown how capping is directed to nascent Pol2 transcripts via physical interactions of one or more of the capping enzymes with the carboxyl-terminal domain (CTD) of the Pol2 Rpb1 subunit.
Dynamic phosphorylation patterns of serine residues in CTD during gene transcription coordinate the recruitment of factors to the elongating RNAPII and to the nascent transcript.
Recent studies identified threonine 4 and tyrosine 1 as new CTD modifications and thereby expanded the “CTD code”.
In this review, we focus on CTD phosphorylation and its function in the RNAPII transcription cycle.
We also discuss in detail the limitations of the phosphospecific CTD antibodies, which are used in all studies.
► The CTD phospho-code is complete with Tyr1-P, Ser2-P, Thr4-P, Ser5-P, and Ser7-P.