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J Biol Chem, Vol. 274, Issue 2, 814-824, January 8, 1999
S-Adenosylmethionine-dependent
Methylation in Saccharomyces cerevisiae
IDENTIFICATION OF A NOVEL PROTEIN ARGININE
METHYLTRANSFERASE
Agnieszka
Niewmierzycka and
Steven
Clarke
From the Department of Chemistry and Biochemistry and the Molecular
Biology Institute, University of California,
Los Angeles, California 90095-1569
We used sequence motifs conserved in
S-adenosylmethionine-dependent methyltransferases
to identify 26 putative methyltransferases from the complete genome of
the yeast Saccharomyces cerevisiae. Seven sequences with
the best matches to the methyltransferase consensus motifs were
selected for further study. We prepared yeast disruption mutants of
each of the genes encoding these sequences, and we found that
disruption of the YJL125c gene is lethal, whereas disruptions of YCR047c and YDR140w lead to slow
growth phenotypes. Normal growth was observed when the YDL201w,
YDR465c, YHR209w, and YOR240w genes were disrupted.
Initial analysis of protein methylation patterns of all mutants by
amino acid analysis revealed that the YDR465c mutant has a
defect in the methylation of the -nitrogen atom of arginine
residues. We propose that YDR465c codes for the
methyltransferase responsible for this recently characterized type of
protein methylation, and we designate the enzyme as Rmt2 (protein
arginine methyltransferase). In
addition, we show that the methylation of susceptible residues in Rmt2
substrates is likely to take place on nascent polypeptide chains and
that these substrates exist in the cell as fully methylated species. Interestingly, Rmt2 has 27% sequence identity over 138 amino acids to
the mammalian guanidinoacetate N-methyltransferase, an
enzyme responsible for methylating the -nitrogen of the small
molecule guanidinoacetate.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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