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Eukaryotic Cell, July 2007, p. 1119-1129, Vol. 6, No. 7
1535-9778/07/$08.00+0     doi:10.1128/EC.00074-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Protein Arginine Methylation in Candida albicans: Role in Nuclear Transport

Anne E. McBride,^1* Cecilia Zurita-Lopez,² Anthony Regis,¹ Emily Blum,¹ Ana Conboy,¹ Shannon Elf,¹ and Steven Clarke²

Department of Biology, Bowdoin College, Brunswick, Maine 04011,¹ Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095²

Received 9 March 2007/ Accepted 30 April 2007

Protein arginine methylation plays a key role in numerous eukaryotic processes, such as protein transport and signal transduction. In Candida albicans, two candidate protein arginine methyltransferases (PRMTs) have been identified from the genome sequencing project. Based on sequence comparison, C. albicans candidate PRMTs display similarity to Saccharomyces cerevisiae Hmt1 and Rmt2. Here we demonstrate functional homology of Hmt1 between C. albicans and S. cerevisiae: CaHmt1 supports growth of S. cerevisiae strains that require Hmt1, and CaHmt1 methylates Npl3, a major Hmt1 substrate, in S. cerevisiae. In C. albicans strains lacking CaHmt1, asymmetric dimethylarginine and -monomethylarginine levels are significantly decreased, indicating that Hmt1 is the major C. albicans type I PRMT1. Given the known effects of type I PRMTs on nuclear transport of RNA-binding proteins, we tested whether Hmt1 affects nuclear transport of a putative Npl3 ortholog in C. albicans. CaNpl3 allows partial growth of S. cerevisiae npl3 strains, but its arginine-glycine-rich C terminus can fully substitute for that of ScNpl3 and also directs methylation-sensitive association with ScNpl3. Expression of green fluorescent protein-tagged CaNpl3 proteins in C. albicans strains with and without CaHmt1 provides evidence for CaHmt1 facilitating export of CaNpl3 in this fungus. We have also identified the C. albicans Rmt2, a type IV fungus- and plant-specific PRMT, by amino acid analysis of an rmt2/rmt2 strain, as well as biochemical evidence for additional cryptic PRMTs.

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* Corresponding author. Mailing address: Department of Biology, 6500 College Station, Bowdoin College, Brunswick, ME 04011. Phone: (207) 798-7109. Fax: (207) 725-3405. E-mail: amcbride{at}bowdoin.edu

Published ahead of print on 4 May 2007.

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Eukaryotic Cell, July 2007, p. 1119-1129, Vol. 6, No. 7
1535-9778/07/$08.00+0     doi:10.1128/EC.00074-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

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