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Nature:组蛋白H2B的糖基化

  1. Nature
  2. 糖基化
  3. 组蛋白

来源:natureasia 2011-12-22 15:22

12月22日,国际著名杂志Nature刊登了研究人员的最新研究成果“GlcNAcylation of histone H2B facilitates its monoubiquitination。”研究揭示,翻译后组蛋白修饰在转录调控中会有重要作用。

12月22日,国际著名杂志Nature刊登了研究人员的最新研究成果“GlcNAcylation of histone H2B facilitates its monoubiquitination。”研究揭示,翻译后组蛋白修饰在转录调控中会有重要作用。

在这项研究中,组蛋白H2B被发现是通过O-linked N-acetylglucosamine (O-GlcNAc)的添加被修饰的,以对细胞外的葡萄糖做出反应。H2B在 Ser112上发生的GlcNAcylation帮助组蛋白在Lys120发生“单泛素化”(monoubiquitylation)。H2B“泛素化”以前曾被发现与活性转录有关。H2B的GlcNAcylation也许会因为有葡萄糖的存在而能帮助基因表达。(生物谷Bioon.com)

GlcNAcylation of histone H2B facilitates its monoubiquitination

Ryoji Fujiki, Waka Hashiba, Hiroki Sekine,Atsushi Yokoyama, Toshihiro Chikanishi, Saya Ito, Yuuki Imai,Jaehoon Kim,Housheng Hansen He,Katsuhide Igarashi,Jun Kanno, Fumiaki Ohtake, Hirochika Kitagawa,Robert G. Roeder, Myles Brown & Shigeaki Kato

Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA1, 2. These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes3, 4. However, the molecular mechanisms that coordinate histone modification patterns remain largely unknown. In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)5, 6. However, the significance of GlcNAcylation in chromatin reorganization remains elusive. Here we report that histone H2B is GlcNAcylated at residue S112 by OGT in vitro and in living cells. Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP)5, 6. H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase. H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes. In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination. These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.

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