Nucleic Acids Research, Vol 26, Issue 3 847-853, Copyright © 1998 by Oxford University Press
AS Neish, SF Anderson, BP Schlegel, W Wei and JD Parvin
The RNA polymerase II (Pol II) holoenzyme in yeast is an essential
transcriptional regulatory complex which has been defined by genetic and
biochemical approaches. The mammalian counterpart to this complex, however,
is less well defined. Experiments herein demonstrate that, along with Pol
II and SRB proteins, proteins associated with transcriptional regulation as
cofactors are associated with the Pol II holoenzyme. Earlier experiments
have demonstrated that the breast cancer-associated tumor suppressor BRCA1
and the CREB binding protein (CBP) were associated with the holoenzyme
complex. The protein related to CBP, the E1A-associated p300 protein, is
shown in these experiments to be associated with the holoenzyme complex as
well as the BRG1 subunit of the chromatin remodeling SWI/SNF complex.
Importantly, the Pol II holoenzyme complex does not contain some factors
previously reported as stoichiometric components of the holoenzyme complex,
most notably the proteins which function in repair of damaged DNA, such as
PCNA, RFC and RPA. The presence of the p300 coactivator and the
chromatin-modifying BRG1 protein support a role for the Pol II holoenzyme
as a key target for regulation by enhancer binding proteins.
ARTICLES
Factors associated with the mammalian RNA polymerase II holoenzyme
Division of Molecular Oncology, Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA.
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