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Eukaryotic Cell, June 2002, p. 448-457, Vol. 1, No. 3
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.3.448-457.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Divergent Subunit Interactions among Fungal mRNA 5'-Capping Machineries

Toshimitsu Takagi,1,{dagger} Eun-Jung Cho,1,2 Rozmin T. K. Janoo,3 Vladimir Polodny,1 Yasutaka Takase,1,{ddagger} Michael-C. Keogh,1 Sue-Ann Woo,1,§ Lucille D. Fresco-Cohen,1 Charles S. Hoffman,3 and Stephen Buratowski1*

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115,1 Department of Biochemistry and Molecular Biology, College of Pharmacy, Sungkyunkwan University, Suwon, Korea,2 Biology Department, Boston College, Chestnut Hill, Massachusetts 024673

Received 18 March 2002/ Accepted 25 March 2002

The Saccharomyces cerevisiae mRNA capping enzyme consists of two subunits: an RNA 5'-triphosphatase (RTPase) and GTP::mRNA guanylyltransferase (GTase). The GTase subunit (Ceg1) binds to the phosphorylated carboxyl-terminal domain of the largest subunit (CTD-P) of RNA polymerase II (pol II), coupling capping with transcription. Ceg1 bound to the CTD-P is inactive unless allosterically activated by interaction with the RTPase subunit (Cet1). For purposes of comparison, we characterize here the related GTases and RTPases from the yeasts Schizosaccharomyces pombe and Candida albicans. Surprisingly, the S. pombe capping enzyme subunits do not interact with each other. Both can independently interact with CTD-P of pol II, and the GTase is not repressed by CTD-P binding. The S. pombe RTPase gene (pct1+) is essential for viability. Pct1 can replace the S. cerevisiae RTPase when GTase activity is supplied by the S. pombe or mouse enzymes but not by the S. cerevisiae GTase. The C. albicans capping enzyme subunits do interact with each other. However, this interaction is not essential in vivo. Our results reveal an unexpected diversity among the fungal capping machineries.

* Corresponding author. Mailing address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115. Phone: (617) 432-0696. Fax: (617) 738-0516. E-mail: steveb{at}hms.harvard.edu.

{dagger} Present address: Department of Automated Biotechnology, Merck Research Labs, North Wales, PA 19454.

{ddagger} Present address: Laboratory of Seeds Finding Technology, Eisai Co. Ltd., Ibaraki 300-2635, Japan.

§ Present address: Department of Cell Biology, Harvard Medical School, Boston, MA 02115.

Eukaryotic Cell, June 2002, p. 448-457, Vol. 1, No. 3
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.3.448-457.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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