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These results suggest that RPAP2 (show RPAP2 Proteins) controls Pol II activity through a direct interaction with Rpb6
Solution structure of the hRPABC14.4 subunit of human RNA polymerases.(RPABC14.4 ?)
POLR2F and PRNP (show PRNP Proteins) exhibited elevated levels in carcinomas compared to normal tissue samples suggesting a possible role for these molecules in colorectal cancer.
The results show that the sites of Pol II pausing and processing factor recruitment change depending on which poly(A) site is utilized. The extent of Pol II C-terminal domain Ser2 (show JAG2 Proteins) phosphorylation does not closely correlate with poly(A) site selection.
Data suggests that DNA methylation (show HELLS Proteins) can be compatible with Pol II binding at selected genes and Pol II stalling can act as alternate mechanism to explain transcriptional silencing associated with DNA methylation (show HELLS Proteins).
This gene encodes the sixth largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes, that is also shared by the other two DNA-directed RNA polymerases. In yeast, this polymerase subunit, in combination with at least two other subunits, forms a structure that stabilizes the transcribing polymerase on the DNA template.
DNA directed RNA polymerase II 14.4 kda polypeptide
, DNA-directed RNA polymerase II subunit F
, DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide
, DNA-directed RNA polymerases I, II, and III subunit RPABC2
, RNA Polymerase II subunit 14.4 kD
, RNA polymerases I, II, and III subunit ABC2
, RPB6 homolog
, RNA Pol II
, polymerase II
, DNA directed RNA polymerase II polypeptide F