Nucleic Acids Research, Vol 24, Issue 19 3771-3777, Copyright © 1996 by Oxford University Press
MO Gold, JP Tassan, EA Nigg, AP Rice and CH Herrmann
Previously, we showed that the viral transactivator proteins E1A and VP16
specifically interact with a cellular CTD kinase activity in vitro. We now
report that E1A and VP16 complexes contain human CDK8, a newly identified
member of the cyclin-dependent kinase family that has been shown to be a
component of the RNA polymerase II (RNAP II) holoenzyme complex. The
presence of CDK8 in the E1A- and VP16- containing complexes is specific for
a functional activation domain of these viral transactivators, strongly
suggesting that this association is relevant for the transactivation
function of E1A and VP16. We show that CDK8 is associated with CTD kinase
activity and that CDK8 co- fractionates with E1A- and VP16-associated CTD
kinase activity over several chromatography columns. Therefore, CDK8 is
likely responsible for the E1A- and VP16-associated CTD kinase activity.
Gel filtration chromatography indicates that the E1A- and VP16-associated
CTD kinase activity has a molecular size of approximately 1.5 MDa and
contains cyclin C and the human homolog of SRB7 in addition to CDK8. This
implies that E1A and VP16 associate with the RNAP II holoenyzme. We also
looked at the transcriptional activity of CDK8 and found that CDK8 can
function as a transcriptional activator when fused to the DNA binding
domain of GAL4. Surprisingly, the ability of GAL4-CDK8 to activate
transcription in this assay was not dependent on the kinase activity of
CDK8, since a kinase-deficient mutant of CDK8 stimulated transcription
nearly as well as wild-type GAL4-CDK8. This suggests that CDK8 may play a
role in transcription that is distinct from its ability to function as a
CTD kinase.
ARTICLES
Viral transactivators E1A and VP16 interact with a large complex that is associated with CTD kinase activity and contains CDK8
Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, USA.
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