Purification and characterization of an RNA polymerase II phosphatase from yeast.

@article{Chambers1996PurificationAC,
  title={Purification and characterization of an RNA polymerase II phosphatase from yeast.},
  author={R Steven Chambers and Caroline M. Kane},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 40},
  pages={24498-504}
}
RNA polymerase (RNAP) II is subject to extensive phosphorylation on the heptapeptide repeats of the C-terminal domain (CTD) of the largest subunit. An activity that is required for the dephosphorylation of yeast RNAP II in vitro has been purified from a yeast whole cell extract by >30,000-fold. The yeast CTD phosphatase activity copurified with two bands with apparent molecular masses of 100 and 103 kDa. The properties of the yeast CTD phosphatase are similar to those of a previously… CONTINUE READING

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