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J. Biol. Chem., Vol. 278, Issue 28, 26078-26085, July 11, 2003
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¶
From the
Department of Medicine, University of
California San Diego, La Jolla, California 92093-0650 and the
Section of Molecular and Cellular Biology,
Division of Biological Sciences, University of California Davis, Davis,
California 95616
The transcription and processing of pre-mRNA in eukaryotic cells are regulated in part by reversible phosphorylation of the C-terminal domain of the largest RNA polymerase (RNAP) II subunit. The CTD phosphatase, FCP1, catalyzes the dephosphorylation of RNAP II and is thought to play a major role in polymerase recycling. This study describes a family of small CTD phosphatases (SCPs) that preferentially catalyze the dephosphorylation of Ser5 within the consensus repeat. The preferred substrate for SCP1 is RNAP II phosphorylated by TFIIH. Like FCP1, the activity of SCP1 is enhanced by the RAP74 subunit of TFIIF. Expression of SCP1 inhibits activated transcription from a number of promoters, whereas a phosphatase-inactive mutant of SCP1 enhances transcription. Accordingly, SCP1 may play a role in the regulation of gene expression, possibly by controlling the transition from initiation/capping to processive transcript elongation.
Received for publication, February 19, 2003 , and in revised form, April 24, 2003.
The nucleotide sequence(s) reported in this paper has been submitted to
the GenBankTM/EBI Data Bank with accession number(s) AY 279529
(SCP1), AY 279530 (SCP1 214), AY279531
* These studies were supported by National Institutes of Health Grants DK13149 (to G. N. G.) and GM33300 (to M. E. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ To whom correspondence should be addressed: University of California San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0650. E-mail: ggill{at}ucsd.edu.
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