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-Human DMA methyltransferase 3 is located in the nucleoli, and its nucleolar localization is mediated by an arginine-rich transcription element.
Human DMA methyltransferase 3 (HsDMAP3) is a newly identified nuclear enzyme that catalyzes the transfer of the symmetric dimethyl moiety from S-adenosyl-L-methionine to the C-5 position of cytosine within the dinucleotides. To understand the mechanism of its nucleolar targeting, chimeric proteins, comprising full-length HsDMAP3 and a variety of deletions, were expressed and their nuclear localization was examined. This showed that a core region of 220 amino acids is responsible for nucleolar targeting. By means of this region, a putative nucleolar localization signal (NoLS) was identified as ARGRNTS. A single deletion mutant of this region (amino acids 218-232) did not localize to nucleoli and its mobility in SDS-PAGE appeared slower than the mobility of the full-length protein. All of these observations strongly suggest that the nucleolar localization of HsDMAP3 is due to the binding of a molecule containing its NoLS with a nucleolar protein, and this is mediated by an arginine-rich transcription element.Q:

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