Cloning of a mammalian DNA methyltransferase.
Cloning and sequencing of cDNA clones has shown that mammalian DNA (cytosine-5)-methyltransferase comprises a 1000-amino acid (aa) N-terminal region of unknown function and a 570-aa C-terminal region that is clearly related to bacterial type-II cytosine restriction methyltransferases. These findings indicate that the mammalian enzyme contains at least two structural domains and suggest a common evolutionary origin for mammalian and prokaryotic DNA (cytosine-5)-methyltransferases.
Bestor
T H
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Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, MA 02115.
D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics; D004247:DNA / Q000235:genetics; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000235:genetics*; D015257:DNA-Cytosine Methylases / Q000235:genetics; D005622:Friend murine leukemia virus; D004915:Leukemia, Erythroblastic, Acute / Q000201:enzymology / Q000235:genetics; D051379:Mice / Q000235:genetics*; D009363:Neoplasm Proteins / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013379:Substrate Specificity
D001426:Bacterial Proteins; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; D004247:DNA; D015257:DNA-Cytosine Methylases; D004248:DNA (Cytosine-5-)-Methyltransferases