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The RAG1 V(D)J recombinase/ubiquitin ligase promotes ubiquitylation of acetylated, phosphorylated histone 3.3

  1. Author:
    Jones, J. M.
    Bhattacharyya, A.
    Simkus, C.
    Vallieres, B.
    Veenstra, T. D.
    Zhou, M.

  2. Author Address

    [Jones, JM; Bhattacharyya, A; Simkus, C; Vallieres, B] Georgetown Univ, Dept Biochem Mol & Cell Biol, Washington, DC 20057 USA [Veenstra, TD; Zhou, M] NCI, Lab Prote & Analyt Technol, Adv Technol Program, SAIC Frederick Inc, Frederick, MD 21702 USA;Jones, JM (reprint author), Georgetown Univ, Dept Biochem Mol & Cell Biol, 3900 Reservoir Rd NW,Basic Sci Bldg,Room 329, Washington, DC 20057 USA;jonesj5@georgetown.edu
    1. Year: 2011
    2. Date: May
  2. Journal: Immunology Letters
    1. 136
    2. 2
    3. Pages: 156-162
  4. Type of Article: Article
  5. ISSN: 0165-2478
  1. Abstract:

    Histone variant H3.3 is associated with transcriptionally active chromatin and accumulates at loci undergoing preparation for V(D)J recombination, a DNA rearrangement required for the assembly of antigen receptors and development of B and T lymphocytes. Here we demonstrate that the RAG1 V(D)J recombinase protein promotes ubiquitylation of H3.3 that has been heavily acetylated and phosphorylated on serine 31 (acetyl-H3.3 S31 p). A fragment of RAG1 promoted formation of a mono-ubiquitylated H3 product that was identified using mass spectrometry as ubiquitylated acetyl-H3.3 S31p. H3 was ubiquitylated at multiple lysine residues, and correspondingly, di-, tri- and higher-order ubiquitylated products were detected at low levels. Ubiquitylation was dependent on an intact RAG1 RING finger/ubiquitin ligase domain and required additional regions of the RAG1 amino terminus that are likely to interact with H3. Acetylated residues within the H3 amino terminal tail were also required. Purified, recombinant H3.1 and H3.3 were not good substrates, suggesting that post-translational modifications enhance recognition by RAG1. A complex including damage-DNA binding protein has also been shown to ubiquitylate H3 in response to UV treatment, suggesting the H3 ubiquitylation may be a common step in multiple DNA repair pathways. (C) 2011 Elsevier B.V. All rights reserved.

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External Sources

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  2. DOI: 10.1016/j.imlet.2011.01.005
  3. View record in Web of Science®
  4. WOS: 000289820200006

Library Notes

  1. Fiscal Year: FY2010-2011
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