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Methyltransferase homology

Baetge, E. E., Suh, Y. H. and Joh, T. H. Complete nucleotide and deduced amino acid sequence of bovine phenylethanolamine N-methyltransferase partial amino acid homology with rat tyrosine hydroxylase. Proc. Natl Acad. Sci. U.S.A. 83 5454-5458,1986. [Pg.223]

The human homolog of yeast Dotl, hDOTlL, is also aH3 K79 specific methyltransferase, and recent studies relate this protein to cancer hDOTlL physically interacts with AFIO, which is an MLL fusion partner in certain leukemias (Okada et al, 2005). [Pg.408]

PRMTl, a nuclear receptor coactivator, exists as in a 330 kDa complex and is a H4 Arg-3 methyltransferase [133,215]. The enzyme appears to be a chromatin bound, and evidence from immunodepletion and knockout studies suggest that it is the principle, if not sole, H4 Arg-3 methyltransferase [133,215]. Mutation of the S-adenosyl methionine binding site in PRMTl annihilated its nuclear receptor coactivator activity with the androgen receptor, providing evidence for the importance of the methylation event in gene expression [215]. Yeast Rmtl, which is homologous to human PRMTl, methylates Arg-3 only in free H4 [208]. [Pg.225]

How are the differential patterns of methylation in the imprinted alleles established and maintained Some evidence exists that differential methylation at the paternal and maternal imprinted alleles are established independently. Knockout of Dnmt3L, a protein that shares homology with de novo DNA methyl-transferase enzymes but does not possess methyltransferase activity, results in a complete loss of the maternally imprinted DNA methylation marks [57,58]. The precise mechanisms by which the paternal methylation imprints are established are yet to be determined. [Pg.327]

Siedlecki, P., Boy, R.G., Comagic, S., Schirrmacher, R., Wiessler, M., Zielenkiewicz, P., Suhai, S. and Lyko, F. (2003) Establishment and functional validation of a structural homology model for human DNA methyltransferase 1. Biochemical and Biophysical Research Communications, 306, 558-563. [Pg.81]

The first committed step in TA and nicotine biosynthesis is catalyzed by putrescine JV-methyltransferase (PMT) (Fig.7.4).82 A PMT cDNA isolated from tobacco showed extensive homology to spermidine synthase from mammalian and bacterial sources.83 A-Methylputrescine is oxidatively deaminated to 4-aminobutanal, which undergoes spontaneous cyclization to form the reactive A-methyl-A1-pyrrolinium cation. Although the enzymes involved are unknown, the A-methyl-A1-pyrrolinium cation is thought to condense either with acetoacetic acid to yield hygrine as a precursor to the tropane ring, or with nicotinic acid to form nicotine. [Pg.152]


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See also in sourсe #XX -- [ Pg.286 ]




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