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Vol. 12, No. 5, pp. 679-691, March 1, 1998
Department of Biological Chemistry and Molecular Pharmacology,
Harvard Medical School, and Dana Farber Cancer Institute,
Boston, Massachusetts 02115 USA
Eukaryotic mRNA processing and export is mediated by various
heterogeneous nuclear ribonucleoproteins (hnRNPs). Many of these hnRNPs
are methylated on arginine residues. In the yeast, Saccharomyces cerevisiae, the predominant enzyme responsible for arginine
methylation is Hmt1p. Hmt1p methylates both Npl3p and Hrp1p, which are
shuttling hnRNPs involved in mRNA processing and export. Here, we
employ an in vivo nuclear export assay to show that arginine
methylation is important for the nuclear export of these hnRNPs. Both
Npl3p and Hrp1p fail to exit the nucleus in cells lacking Hmt1p, and overexpression of Hmt1p enhances Npl3p export. The export of a novel
hnRNP-like protein, Hrb1p, which does not bind poly(A)+ RNA,
however, is not affected by the lack of methylation. Furthermore, we
find a genetic relationship between Hmt1p and cap-binding protein 80 (CBP80). Together, these findings establish that one
biological role for arginine methylation is in facilitating the export
of certain hnRNPs out of the nucleus.
[Key Words: HMT1; NPL3; HRP1; CBP80; heterogeneous ribonucleoprotein (hnRNP); arginine methylation; mRNA export]
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