The d-isoAsp-25 variant of histone H2B is highly enriched in active chromatin: potential role in the regulation of gene expression?

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• 作者：Zhenxia Qin ; Jeff X. Zhu ; Dana W. Aswad
• 关键词：d ; Aspartate ; Chromatin ; Histone ; Isoaspartate ; Isomerization ; Methylation
• 刊名：Amino Acids
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：48
• 期：2
• 页码：599-603
• 全文大小：593 KB
• 参考文献：Aswad DW, Paranandi MV, Schurter BT (2000) Isoaspartate in peptides and proteins: formation, significance, and analysis. J Pharm Biomed Anal 21:1129–1136CrossRef PubMed
  Clarke S (1987) Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int J Peptide Protein Res 30:808–821CrossRef
  Johnson BA, Murray ED Jr, Clarke S, Glass DB, Aswad DW (1987) Protein carboxyl methyltransferase facilitates conversion of atypical l -isoaspartyl peptides to normal l -aspartyl peptides. J Biol Chem 262:5622–5629PubMed
  Khoury MK, Parker I, Aswad DW (2010) Acquisition of chemiluminescent signals from immunoblots with a digital single-lens reflex camera. Anal Biochem 397:129–131PubMedCentral CrossRef PubMed
  Kim E, Lowenson JD, MacLaren DC, Clarke S, Young SG (1997) Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice. Proc Natl Acad Sci USA 94:6132–6137PubMedCentral CrossRef PubMed
  McFadden PN, Clarke S (1987) Conversion of isoaspartyl peptides to normal peptides: implications for the cellular repair of damaged proteins. Proc Natl Acad Sci USA 84:2595–2599PubMedCentral CrossRef PubMed
  Sydow JF et al (2014) Structure-based prediction of asparagine and aspartate degradation sites in antibody variable regions. PLoS One 9:e100736PubMedCentral CrossRef PubMed
  Venkatesh S, Workman JL (2015) Histone exchange, chromatin structure and the regulation of transcription. Nat Rev Mol Cell Biol 16:178–189CrossRef
  Young AL, Carter WG, Doyle HA, Mamula MJ, Aswad DW (2001) Structural integrity of histone H2B in vivo requires the activity of protein l -isoaspartate O-methyltransferase, a putative protein repair enzyme. J Biol Chem 276:37161–37165CrossRef PubMed
  Young GW, Hoofring SA, Mamula MJ, Doyle HA, Bunick GJ, Hu Y, Aswad DW (2005) Protein L-isoaspartyl methyltransferase catalyzes in vivo racemization of Aspartate-25 in mammalian histone H2B. J Biol Chem 280:26094–26098CrossRef PubMed
  
• 作者单位：Zhenxia Qin (1) (2)
  Jeff X. Zhu (1) (3)
  Dana W. Aswad (1)
  
  1. Department of Molecular Biology and Biochemistry, University of California, 3205 McGaugh Hall, Irvine, CA, 92697-3900, USA
  2. Department of Anatomy, School of Basic Medicine, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China
  3. USP-China, No. 520 North Fute Road, Waigaoqlao Free Trade Zone, Shanghai, 200131, China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Analytical Chemistry
  Biochemical Engineering
  Life Sciences
  Proteomics
  Neurobiology
  
• 出版者：Springer Wien
• ISSN：1438-2199

文摘

Approximately 12 % of histone H2B in mammalian brain contains an unusual d-aspartate residue in its N-terminal tail. Most of this d-aspartate is linked to the C-flanking glycine via an isopeptide bond. To explore the possible significance of these modifications, we generated an antibody to the d-isoaspartyl form of H2B, and used it to assess its levels in H2B associated with “active” vs. “silent” chromatin. We found that the d-isoaspartyl form of H2B appears to be highly enriched in the former. This irreversible modification could serve a novel regulatory function in gene expression.