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Histone H3K4 methylation keeps centromeres open for business
Author(s) -
Stimpson Kaitlin M,
Sullivan Beth A
Publication year - 2011
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2010.339
Subject(s) - biology , centromere , histone , histone methylation , genetics , histone methyltransferase , dna methylation , microbiology and biotechnology , chromosome , dna , gene expression , gene
Nucleosomes at eukaryotic centromeres combine the histone H3 variant CENP‐A and canonical H3 di‐methylated at lysine 4 (H3K4me2), whose functional importance within the centromere region remains elusive. In this issue, Bergmann et al reveal a role for H3K4me2 in CENP‐A maintenance, and extend the profile of centromeric histone modifications to include H3K36 methylation, typically found in transcribed regions of the genome.

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