ArticleDevelopmental and comparative immunology2008
The PHD domain of the sea urchin RAG2 homolog, SpRAG2L, recognizes dimethylated lysine 4 in histone H3 tails.
Article in Developmental and comparative immunology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Insights into RAG Evolution from the Identification of "Missing Link" Family A RAGL Transposons.Molecular biology and evolution · 2023Article
- Structural insights into the evolution of the RAG recombinase.Nature reviews. Immunology · 2022Review
- Different sea urchin RAG-like genes were domesticated to carry out different functions.Frontiers in immunology · 2022Article
- Guardian of the Genome: An Alternative RAG/Transib Co-Evolution Hypothesis for the Origin of V(D)J Recombination.Frontiers in immunology · 2021Article
- Identification of RAG-like transposons in protostomes suggests their ancient bilaterian origin.Mobile DNA · 2020Article
- New insights into the evolutionary origins of the recombination-activating gene proteins and V(D)J recombination.The FEBS journal · 2017Review
- Phf7 controls male sex determination in the Drosophila germline.Developmental cell · 2012Article
- The origins of vertebrate adaptive immunity.Nature reviews. Immunology · 2010Review
- Construction of a medicinal leech transcriptome database and its application to the identification of leech homologs of neural and innate immune genes.BMC genomics · 2010Article
- The origins of the Rag genes--from transposition to V(D)J recombination.Seminars in immunology · 2010Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
V(D)J recombination is a somatic gene rearrangement process that assembles antigen receptor genes from individual segments during lymphocyte development. The access of the RAG1/RAG2 recombinase to these gene segments is regulated at the level of chromatin modifications, in particular histone tail modifications. Trimethylation of lysine 4 in histone H3 (H3K4me3) correlates with actively recombining gene elements, and this mark is recognized and interpreted by the plant homeodomain (PHD) of RAG2. Here we report that the PHD domain of the only known invertebrate homolog of RAG2, the SpRAG2L protein of the purple sea urchin (Strongylocentrotus purpuratus) also binds to methylated histones, but with a unique preference for H3K4me2. While the cognate substrate for the sea urchin RAG1L/RAG2L complex remains elusive, the affinity for histone tails and the nuclear localization of ectopically expressed SpRAG2L strongly support the model that this enzyme complex exerts its activity on DNA in the context of chromatin.
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