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Molecular and Cellular Biology, May 2007, p. 3601-3611, Vol. 27, No. 10
0270-7306/07/$08.00+0 doi:10.1128/MCB.02187-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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Max F. Perutz Laboratories, Medical University of Vienna, Department of Medical Biochemistry, Bohrgasse 9/3, A-1030 Vienna, Austria,1 Sir William Dunn School of Pathology, Department of Biochemistry, University of Oxford, Oxford, United Kingdom2
Received 22 November 2006/ Returned for modification 3 January 2007/ Accepted 26 February 2007
Phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates transcription and coordinates it with pre-mRNA processing. We show here that Rct1, a nuclear multidomain cyclophilin from Schizosaccharomyces pombe, is encoded by an essential gene that interacts with the CTD and regulates its phosphorylation in vivo. Downregulation of Rct1 levels results in increased phosphorylation of the CTD at both Ser2 and Ser5 and in a commensurate decrease in RNAP II transcription. In contrast, overexpression of Rct1 decreases phosphorylation on both sites. The close association of Rct1 with transcriptionally active chromatin suggests a role in regulation of RNAP II transcriptional activity. These data, together with the pleiotropic phenotype upon Rct1 deregulation, suggest that this multidomain cyclophilin is an important player in maintaining the correct phosphorylation code of the CTD and thereby regulating CTD function.
Published ahead of print on 5 March 2007.
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