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J. Biol. Chem., Vol. 269, Issue 42, 26243-26248, 10, 1994
RS Chambers and ME Dahmus
The repetitive C-terminal domain (CTD) of RNA polymerase (RNAP) II is
extensively phosphorylated concomitant with the initiation of transcription
and must be dephosphorylated before RNAP II can begin another round of
transcription. A CTD phosphatase was purified more than 7,500-fold from a
HeLa cell extract. SDS-polyacrylamide gel electrophoresis shows a
predominant protein of 205 kDa and a less abundant protein of 150 kDa
co-eluting with the CTD phosphatase activity. Sedimentation and gel
filtration analysis suggest that CTD phosphatase has an elongated structure
with a M(r) of 200,000. This enzyme is a type 2C phosphatase in that it
requires Mg2+ for activity and is resistant to okadaic acid. CTD
phosphatase appears to processively dephosphorylate the CTD and is specific
in that it does not dephosphorylate phosphorylase a, the alpha or beta
subunits of phosphorylase kinase or RNAP II phosphorylated with casein
kinase II. CTD phosphatase dephosphorylates RNAP IIO purified from calf
thymus or generated in vitro by two previously described CTD kinases. These
results suggest that CTD phosphatase has the properties expected for a
protein phosphatase that catalyzes the conversion of RNAP IIO to RNAP IIA
and may play a key role in the transcription cycle of RNAP II.
Purification and characterization of a phosphatase from HeLa cells which dephosphorylates the C-terminal domain of RNA polymerase II
Section of Molecular and Cellular Biology, University of California, Davis 95616.
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