Histone Methylation is Making its Mark

Data derived from the Science Watch/Hot Papers database and the Web of Science (ISI, Philadelphia) show that Hot Papers are cited 50 to 100 times more often than the average paper of the same type and age. M. Lachner et al., "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins," Nature, 410:116-20, 2001. (Cited in 202 papers) A.J. Bannister et al., "Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain," Nature, 410:120-4, 2001. (Cited in 2

Written byBrendan Maher
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Beyond A, C, T, and G lies an epigenetic level of heritable control that has reached the forefront of biomedical research. Histone modification patterns, like multicolored highlighting in the genome's book of life, tell eukaryotic cells when to turn genes on and off, thus making sense of its DNA instructions. In 1993, researchers first pondered whether these alterations on N-terminal tails of histone proteins created a readable code1 (See also 5-Prime). Eight years later, groups from Austria and the United Kingdom wrote what many consider as the first complete chapter on the histone code hypothesis.2,3

Using mammalian cells and fission yeast, these two groups built on findings that histone methyltransferase SU(VAR)3-9 and its yeast homolog, Clr4, specifically methylate the ninth lysine (K9) on histone H3's tail. This methylated lysine, and none other, acts as a binding site for heterochromatin protein HP1, which was long associated with silent heterochromatic regions of ...

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