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(Received for publication, January 11, 1996; and in revised form, March 4, 1996) We have identified the major enzymatic activity responsible for
the S-adenosyl-L-methionine-dependent methylation of
arginine residues (EC 2.1.1.23) in proteins of the yeast Saccharomyces cerevisiae. The RMT1 (protein-arginine
methyltransferase), formerly ODP1, gene product encodes a
348-residue polypeptide of 39.8 kDa that catalyzes both the N
Volume 271,
Number 21,
Issue of May 24, 1996 pp. 12585-12594
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-mono- and N,N-asymmetric dimethylation
of arginine residues in a variety of endogenous yeast polypeptides. A
yeast strain in which the chromosomal RMT1 gene was disrupted
is viable, but the level of N,N-[
H]dimethylarginine
residues detected in intact cells incubated with S-adenosyl-L-[methyl-H]methionine
is reduced to less than 15% of the levels found in the parent strain,
while the N-[H]monomethylarginine
content is reduced to less than 30%. We show that soluble extract from
parent cells, but not from mutant rmt1 cells, catalyzes the in vitro methylation of endogenous polypeptides of 55, 41, 38,
34, and 30 kDa. The hypomethylated form of these five polypeptides, as
well as that of several others, can be mono- and asymmetrically
dimethylated by incubating the mutant rmt1 extract with a
purified, bacterially produced, glutathione S-transferase-RMT1
fusion protein and S-adenosyl-L-[methyl-H]methionine.
This glutathione S-transferase-RMT1 fusion protein is also
able to methylate a number of mammalian polypeptides including
histones, recombinant heterogeneous ribonucleoprotein A1, cytochrome c, and myoglobin, but cannot methylate myelin basic protein.
RMT1 appears to be a yeast homolog of a recently characterized
mammalian protein-arginine methyltransferase whose activity may be
modulated by mitotic stimulation of cells.
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W.-J. Lin, J. D. Gary, M. C. Yang, S. Clarke, and H. R. Herschman The Mammalian Immediate-early TIS21 Protein and the Leukemia-associated BTG1 Protein Interact with a Protein-arginine N-Methyltransferase J. Biol. Chem., June 21, 1996; 271(25): 15034 - 15044. [Abstract] [Full Text] [PDF]
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H. Brahms, J. Raymackers, A. Union, F. de Keyser, L. Meheus, and R. Luhrmann 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 J. Biol. Chem., May 26, 2000; 275(22): 17122 - 17129. [Abstract] [Full Text] [PDF]
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P. Zobel-Thropp, M. C. Yang, L. Machado, and S. Clarke A Novel Post-translational Modification of Yeast Elongation Factor 1A. METHYLESTERIFICATION AT THE C TERMINUS J. Biol. Chem., November 17, 2000; 275(47): 37150 - 37158. [Abstract] [Full Text] [PDF]
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E. C. Shen, T. Stage-Zimmermann, P. Chui, and P. A. Silver 7The Yeast mRNA-binding Protein Npl3p Interacts with the Cap-binding Complex J. Biol. Chem., July 28, 2000; 275(31): 23718 - 23724. [Abstract] [Full Text] [PDF]
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K. Inoue, T. Mizuno, K. Wada, and M. Hagiwara Novel RING Finger Proteins, Air1p and Air2p, Interact with Hmt1p and Inhibit the Arginine Methylation of Npl3p J. Biol. Chem., October 13, 2000; 275(42): 32793 - 32799. [Abstract] [Full Text] [PDF]
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A. Frankel and S. Clarke PRMT3 Is a Distinct Member of the Protein Arginine N-Methyltransferase Family. CONFERRAL OF SUBSTRATE SPECIFICITY BY A ZINC-FINGER DOMAIN J. Biol. Chem., October 13, 2000; 275(42): 32974 - 32982. [Abstract] [Full Text] [PDF]
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J. Rho, S. Choi, Y. R. Seong, W.-K. Cho, S. H. Kim, and D.-S. Im PRMT5, Which Forms Distinct Homo-oligomers, Is a Member of the Protein-arginine Methyltransferase Family J. Biol. Chem., March 30, 2001; 276(14): 11393 - 11401. [Abstract] [Full Text] [PDF]
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T. L. Branscombe, A. Frankel, J.-H. Lee, J. R. Cook, Z.-h. Yang, S. Pestka, and S. Clarke PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins J. Biol. Chem., August 24, 2001; 276(35): 32971 - 32976. [Abstract] [Full Text] [PDF]
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M. T. Bedford, A. Frankel, M. B. Yaffe, S. Clarke, P. Leder, and S. Richard Arginine Methylation Inhibits the Binding of Proline-rich Ligands to Src Homology 3, but Not WW, Domains J. Biol. Chem., May 19, 2000; 275(21): 16030 - 16036. [Abstract] [Full Text] [PDF]
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