Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 12 February 1971:
Vol. 171. no. 3971, pp. 579 - 581
DOI: 10.1126/science.171.3971.579
Prev | Table of Contents | Next

Articles

Specific Enzymic Methylation of an Arginine in the Experimental Allergic Encephalomyelitis Protein from Human Myelin

G. S. Baldwin 1 and P. R. Carnegie 1

1 Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia

A cytoplasmic enzyme from guinea pig brain was shown to transfer methyl groups from S-adenosylmethionine to only one of 19 arginine residues in the basic protein from human brain. The products were ohgr-N-monomethylarginine and ohgr-N,N'-dimethylarginine. These methylated arginines are adjacent to the main encephalitogenic determinant in the protein. Methylation may aid in the transfer of this region of the protein into the nonpolar environment within myelin and in maintaining the integrity of myelin.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Regulation of heterogenous nuclear ribonucleoprotein A1 transport by phosphorylation in cells stressed by osmotic shock.
E. Allemand, S. Guil, M. Myers, J. Moscat, J. F. Caceres, and A. R. Krainer (2005)
PNAS 102, 3605-3610
   Abstract »    Full Text »    PDF »
Protein Interfaces in Signaling Regulated by Arginine Methylation.
F.-M. Boisvert, C. A. Chenard, and S. Richard (2005)
Sci. STKE 2005, re2
   Abstract »    Full Text »    PDF »
PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine.
J.-H. Lee, J. R. Cook, Z.-H. Yang, O. Mirochnitchenko, S. I. Gunderson, A. M. Felix, N. Herth, R. Hoffmann, and S. Pestka (2005)
J. Biol. Chem. 280, 3656-3664
   Abstract »    Full Text »    PDF »
Treatment of AIDS-associated myelopathy with L-methionine: A placebo-controlled study.
A. Di Rocco, P. Werner, T. Bottiglieri, J. Godbold, M. Liu, M. Tagliati, A. Scarano, and D. Simpson (2004)
Neurology 63, 1270-1275
   Abstract »    Full Text »    PDF »
Small Molecule Regulators of Protein Arginine Methyltransferases.
D. Cheng, N. Yadav, R. W. King, M. S. Swanson, E. J. Weinstein, and M. T. Bedford (2004)
J. Biol. Chem. 279, 23892-23899
   Abstract »    Full Text »    PDF »
Multiple Sclerosis: An Important Role for Post-Translational Modifications of Myelin Basic Protein in Pathogenesis.
J. K. Kim, F. G. Mastronardi, D. D. Wood, D. M. Lubman, R. Zand, and M. A. Moscarello (2003)
Mol. Cell. Proteomics 2, 453-462
   Abstract »    Full Text »    PDF »
In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p.
C. XU, P. A. HENRY, A. SETYA, and M. F. HENRY (2003)
RNA 9, 746-759
   Abstract »    Full Text »    PDF »
Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1.
J. Cote, F.-M. Boisvert, M.-C. Boulanger, M. T. Bedford, and S. Richard (2003)
Mol. Biol. Cell 14, 274-287
   Abstract »    Full Text »
Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing.
F.-M. Boisvert, J. Cote, M.-C. Boulanger, P. Cleroux, F. Bachand, C. Autexier, and S. Richard (2002)
J. Cell Biol. 159, 957-969
   Abstract »    Full Text »    PDF »
Determinants of the Interaction of the Spinal Muscular Atrophy Disease Protein SMN with the Dimethylarginine-modified Box H/ACA Small Nucleolar Ribonucleoprotein GAR1.
S. E. Whitehead, K. W. Jones, X. Zhang, X. Cheng, R. M. Terns, and M. P. Terns (2002)
J. Biol. Chem. 277, 48087-48093
   Abstract »    Full Text »    PDF »
A Novel WD Repeat Protein Component of the Methylosome Binds Sm Proteins.
W. J. Friesen, A. Wyce, S. Paushkin, L. Abel, J. Rappsilber, M. Mann, and G. Dreyfuss (2002)
J. Biol. Chem. 277, 8243-8247
   Abstract »    Full Text »    PDF »
The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity.
A. Frankel, N. Yadav, J. Lee, T. L. Branscombe, S. Clarke, and M. T. Bedford (2002)
J. Biol. Chem. 277, 3537-3543
   Abstract »    Full Text »    PDF »
The Methylosome, a 20S Complex Containing JBP1 and pICln, Produces Dimethylarginine-Modified Sm Proteins.
W. J. Friesen, S. Paushkin, A. Wyce, S. Massenet, G. S. Pesiridis, G. Van Duyne, J. Rappsilber, M. Mann, and G. Dreyfuss (2001)
Mol. Cell. Biol. 21, 8289-8300
   Abstract »    Full Text »    PDF »
Analysis of the Yeast Arginine Methyltransferase Hmt1p/Rmt1p and Its in Vivo Function. COFACTOR BINDING AND SUBSTRATE INTERACTIONS.
A. E. McBride, V. H. Weiss, H. K. Kim, J. M. Hogle, and P. A. Silver (2000)
J. Biol. Chem. 275, 3128-3136
   Abstract »    Full Text »    PDF »
The Human Homologue of the Yeast Proteins Skb1 and Hsl7p Interacts with Jak Kinases and Contains Protein Methyltransferase Activity.
B. P. Pollack, S. V. Kotenko, W. He, L. S. Izotova, B. L. Barnoski, and S. Pestka (1999)
J. Biol. Chem. 274, 31531-31542
   Abstract »    Full Text »    PDF »
Biological significance of endogenous methylarginines that inhibit nitric oxide synthases.
J. Leiper and P. Vallance (1999)
Cardiovasc Res 43, 542-548
   Abstract »    Full Text »    PDF »
The Mammalian Immediate-early TIS21 Protein and the Leukemia-associated BTG1 Protein Interact with a Protein-arginine N-Methyltransferase.
W.-J. Lin, J. D. Gary, M. C. Yang, S. Clarke, and H. R. Herschman (1996)
J. Biol. Chem. 271, 15034-15044
   Abstract »    Full Text »    PDF »
The Predominant Protein-arginine Methyltransferase from Saccharomyces cerevisiae.
J. D. Gary, W.-J. Lin, M. C. Yang, H. R. Herschman, and S. Clarke (1996)
J. Biol. Chem. 271, 12585-12594
   Abstract »    Full Text »    PDF »
Posttranslational covalent modification of proteins.
R Uy and F Wold (1977)
Science 198, 890-896
   Abstract »    PDF »
Myelin Basic Protein: Location of Multiple Independent Antigenic Regions.
B. F. Driscoll, A. J. Kramer, and M. W. Kies (1974)
Science 184, 73-75
   Abstract »    PDF »
The Structure of Biological Membranes: Current Status.
J. D. Robertson (1972)
Arch Intern Med 129, 202-228
   Abstract »    PDF »
Protein Methylation.
W. K. Paik and S. Kim (1971)
Science 174, 114-119
   PDF »
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.
H. Brahms, J. Raymackers, A. Union, F. de Keyser, L. Meheus, and R. Luhrmann (2000)
J. Biol. Chem. 275, 17122-17129
   Abstract »    Full Text »    PDF »
PRMT3 Is a Distinct Member of the Protein Arginine N-Methyltransferase Family. CONFERRAL OF SUBSTRATE SPECIFICITY BY A ZINC-FINGER DOMAIN.
A. Frankel and S. Clarke (2000)
J. Biol. Chem. 275, 32974-32982
   Abstract »    Full Text »    PDF »
PRMT5, Which Forms Distinct Homo-oligomers, Is a Member of the Protein-arginine Methyltransferase Family.
J. Rho, S. Choi, Y. R. Seong, W.-K. Cho, S. H. Kim, and D.-S. Im (2001)
J. Biol. Chem. 276, 11393-11401
   Abstract »    Full Text »    PDF »
Exposure on Cell Surface and Extensive Arginine Methylation of Ewing Sarcoma (EWS) Protein.
L. L. Belyanskaya, P. M. Gehrig, and H. Gehring (2001)
J. Biol. Chem. 276, 18681-18687
   Abstract »    Full Text »    PDF »
PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins.
T. L. Branscombe, A. Frankel, J.-H. Lee, J. R. Cook, Z.-h. Yang, S. Pestka, and S. Clarke (2001)
J. Biol. Chem. 276, 32971-32976
   Abstract »    Full Text »    PDF »
Arginine Methylation Inhibits the Binding of Proline-rich Ligands to Src Homology 3, but Not WW, Domains.
M. T. Bedford, A. Frankel, M. B. Yaffe, S. Clarke, P. Leder, and S. Richard (2000)
J. Biol. Chem. 275, 16030-16036
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)