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(Received for publication, November 7, 1996, and in revised form, February 11, 1997)
From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
Hyperphosphorylation of the C-terminal
heptapeptide repeat domain (CTD) of the RNA polymerase II largest
subunit has been suggested to play a key role in regulating
transcription initiation and elongation. To facilitate investigating
functional consequences of CTD phosphorylation we developed new
templates, the double G-less cassettes, which make it possible to assay
simultaneously the level of initiation and the efficiency of
elongation. Using these templates, we examined the effects of yeast CTD
kinase I or CTD kinase inhibitors on transcription and CTD
phosphorylation in HeLa nuclear extracts. Our results showed that
polymerase II elongation efficiency and CTD phosphorylation are greatly
reduced by CTD kinase inhibitors, whereas both are greatly increased by CTD kinase I; in contrast, transcription initiation is much less affected. These results demonstrate that CTD kinase I modulates the
elongation efficiency of RNA polymerase II and are consistent with the
idea that one function of CTD phosphorylation is to promote effective
production of long transcripts by stimulating the elongation efficiency
of RNA polymerase II.
Volume 272, Number 17,
Issue of April 25, 1997
pp. 10990-10993
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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