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  Spatial Distribution of Di- and Tri-methyl Lysine 36 of Histone H3 at Active Genes

Bannister, A. J., Schneider, R., Myers, F. A., Thorne, A. W., Crane-Robinson, C., & Kouzarides, T. (2005). Spatial Distribution of Di- and Tri-methyl Lysine 36 of Histone H3 at Active Genes. The Journal of Biological Chemistry, 280(18), 17732-17736.

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Bannister, Andrew J., Author
Schneider, Robert1, Author           
Myers, Fiona A., Author
Thorne, Alan W., Author
Crane-Robinson, Colyn, Author
Kouzarides, Tony, Author
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1Spemann Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243655              

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 Abstract: Methylation of lysine 4 of histone H3 (K4/H3) is linked to transcriptional activity, whereas methylation of K9/H3 is tightly associated with gene inactivity. These are well characterized sites of methylation within histones, but there are numerous other, less characterized, sites of modification. In Saccharomyces cerevisiae, methylation of K36/H3 has been linked to active genes, but little is known about this methylation in higher eukaryotes. Here we analyzed for the first time the levels and spatial distribution of di- and tri-methyl (di- and tri-Me) K36/H3 in metazoan genes. We analyzed chicken genes that are developmentally regulated, constitutively active, or inactive. We found that active genes contain high levels of these modifications compared with inactive genes. Furthermore, in actively transcribed regions the levels of di- and tri-Me K36/H3 peak toward the 3' end of the gene. This is in striking contrast to the distributions of di- and tri-Me K4/H3, which peak early in actively transcribed regions. Thus, di/tri-Me K4/H3 and di/tri-Me K36/H3 are both useful markers of active genes, but their genic distribution indicates differing roles. Our data suggest that the unique spatial distribution of di- and tri-Me K36/H3 plays a role in transcriptional termination and/or early RNA processing.

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Language(s): eng - English
 Dates: 2005-05-06
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 250119
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Title: The Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 280 (18) Sequence Number: - Start / End Page: 17732 - 17736 Identifier: -