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

@article{Jones2011TheRV,
  title={The RAG1 V(D)J recombinase/ubiquitin ligase promotes ubiquitylation of acetylated, phosphorylated histone 3.3.},
  author={Jessica M. Jones and Anamika Bhattacharyya and Carrie L Simkus and Brice Vallieres and Timothy D. Veenstra and Ming Zhou},
  journal={Immunology letters},
  year={2011},
  volume={136 2},
  pages={
          156-62
        }
}
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 S31p). A fragment of RAG1 promoted formation of a mono-ubiquitylated H3… CONTINUE READING
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