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Molecular and Cellular Biology, January 2004, p. 846-855, Vol. 24, No. 2
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.2.846-855.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Role of the C-Terminal Domain of RNA Polymerase II in U2 snRNA Transcription and 3' Processing

Erica Y. Jacobs,1 Ikuo Ogiwara,2 and Alan M. Weiner1*

Department of Biochemistry, School of Medicine, University of Washington, Seattle, Washington 98195-7350,1 Laboratory for Neurogenetics, RIKEN Institute, Wako-shi, Saitama 351-0198, Japan2

Received 27 May 2003/ Returned for modification 3 July 2003/ Accepted 15 October 2003

U small nuclear RNAs (snRNAs) and mRNAs are both transcribed by RNA polymerase II (Pol II), but the snRNAs have unusual TATA-less promoters and are neither spliced nor polyadenylated; instead, 3' processing is directed by a highly conserved 3' end formation signal that requires initiation from an snRNA promoter. Here we show that the C-terminal domain (CTD) of Pol II is required for efficient U2 snRNA transcription, as it is for mRNA transcription. However, CTD kinase inhibitors, such as 5,6-dichloro-1-ß-D-ribofuranosylbenzimidazole (DRB) and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H7), that block mRNA elongation do not affect U2 transcription, although 3' processing of the U2 primary transcript is impaired. We show further that U2 transcription is preferentially inhibited by low doses of UV irradiation or actinomycin D, which induce CTD kinase activity, and that UV inhibition can be rescued by treatment with DRB or H7. We propose that Pol II complexes transcribing snRNAs and mRNAs have distinct CTD phosphorylation patterns. mRNA promoters recruit factors including kinases that hyperphosphorylate the CTD, and the CTD in turn recruits proteins needed for mRNA splicing and polyadenylation. We predict that snRNA promoters recruit factors including a CTD kinase(s) whose snRNA-specific phosphorylation pattern recruits factors required for promoter-coupled 3' end formation.

* Corresponding author. Mailing address: Department of Biochemistry, School of Medicine, University of Washington, Seattle, WA 98195-7350. Phone: (206) 543-1768. Fax: (206) 685-9231. E-mail: amweiner{at}u.washington.edu.

Molecular and Cellular Biology, January 2004, p. 846-855, Vol. 24, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.2.846-855.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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