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Originally published In Press as doi:10.1074/jbc.M000300200 on March 19, 2000

J. Biol. Chem., Vol. 275, Issue 22, 17122-17129, June 2, 2000
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The C-terminal RG Dipeptide Repeats of the Spliceosomal Sm Proteins D1 and D3 Contain Symmetrical Dimethylarginines, Which Form a Major B-cell Epitope for Anti-Sm Autoantibodies*

Hero BrahmsDagger §, Jos Raymackers, Ann Union, Filip de Keyser||, Lydie Meheus**, and Reinhard LührmannDagger §**

From the Dagger  Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff-Str. 2, D-35037 Marburg, Germany, the § Max-Planck-Institute of Biophysical Chemistry, Department of Cellular Biochemistry, Am Faßberg 11, D-37070 Göttingen, Germany,  Innogenetics N.V., Industriepark Zwijnaarde 7, Box 4, B-9052 Ghent, Belgium, and the || Department of Rheumatology, Ghent University Hospital, B-9000 Ghent, Belgium

The Sm proteins B/B', D1, D2, D3, E, F, and G are components of the small nuclear ribonucleoproteins U1, U2, U4/U6, and U5 that are essential for the splicing of pre-mRNAs in eukaryotes. D1 and D3 are among the most common antigens recognized by anti-Sm autoantibodies, an autoantibody population found exclusively in patients afflicted with systemic lupus erythematosus. Here we demonstrate by protein sequencing and mass spectrometry that all arginines in the C-terminal arginine-glycine (RG) dipeptide repeats of the human Sm proteins D1 and D3, isolated from HeLa small nuclear ribonucleoproteins, contain symmetrical dimethylarginines (sDMAs), a posttranslational modification thus far only identified in the myelin basic protein. The further finding that human D1 individually overexpressed in baculovirus-infected insect cells contains asymmetrical dimethylarginines suggests that the symmetrical dimethylation of the RG repeats in D1 and D3 is dependent on the assembly status of D1 and D3. In antibody binding studies, 10 of 11 anti-Sm patient sera tested, as well as the monoclonal antibody Y12, reacted with a chemically synthesized C-terminal peptide of D1 containing sDMA, but not with peptides containing asymmetrically modified or nonmodified arginines. These results thus demonstrate that the sDMA-modified C terminus of D1 forms a major linear epitope for anti-Sm autoantibodies and Y12 and further suggest that posttranslational modifications of Sm proteins play a role in the etiology of systemic lupus erythematosus.

* This work was supported in part by a grant from the Deutsche Forschungsgemeinschaft (to R. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence and reprint requests may be addressed: Lydie Meheus, Innogenetics N.V., Industriepark Zwijnaarde 7, Box 4, B-9052 Ghent, Belgium. Tel.: 32-9-2410711; Fax: 32-9-2410907; E-mail: Lydie_Meheus@innogenetics.com or Reinhard Luhrmann, Tel.: 49-551-2011407; Fax: 49-551-2011197; E-mail: R.Luehrmann@gwdg.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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