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J Biol Chem, Vol. 273, Issue 10, 5427-5430, March 6, 1998
From the Department of Biochemistry and Molecular Biology,
University of Kansas Medical Center,
Kansas City, Kansas 66160-7421
The cell cycle is regulated by various
protein kinases, including cyclin-dependent kinases (CDKs).
D-type CDKs, CDK4, and CDK6, phosphorylate retinoblastoma protein and
are believed to regulate through the G1 phase of the
cell cycle. CDK inhibitor p16INK4A has been characterized
as binding CDK4 and CDK6 and as inhibiting phosphorylation of
retinoblastoma protein by these CDKs. Thus p16INK4A is
implicated in regulating the cell cycle at the G1 phase.
The largest subunit of RNA polymerase II (pol II) contains an essential C-terminal domain (CTD). General transcription factor TFIIH, which contains CDK7, phosphorylates the CTD in vitro. The CTD
phosphorylation is shown to be involved in transcriptional regulation
in vivo and in vitro. Phosphorylation of RNA
pol II CTD by TFIIH is thought to play an important role in
transcriptional regulation. Here we report that p16INK4A
associates with RNA pol II CTD and TFIIH. p16INK4A
inhibited the CTD phosphorylation by TFIIH. These findings suggest that
p16INK4A may regulate transcription via CTD phosphorylation
in the cell cycle.
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