Journal
IMMUNITY
Volume 23, Issue 2, Pages 203-212Publisher
CELL PRESS
DOI: 10.1016/j.immuni.2005.07.004
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Funding
- NCI NIH HHS [P30 CA08748] Funding Source: Medline
- NIAID NIH HHS [AI 07605, AI45996, P01 AI61093] Funding Source: Medline
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V(D)J recombination is a tightly controlled process of somatic recombination whose regulation is mediated in part by chromatin structure. Here, we report that RAG2 binds directly to the core histone proteins. The interaction with histones is observed in developing lymphocytes and within the RAG1/RAG2 recombinase complex in a manner that is dependent on the RAG2 C terminus. Amino acids within the plant homeo domain (PHD)-like domain as well as a conserved acidic stretch of the RAG2 C terminus that is considered to be a linker region are important for this interaction. Point mutations that disrupt the RAG2-histone association inhibit the efficiency of the V(D)J recombination reaction at the endogenous immunoglobulin locus, with the most dramatic effect in the V to DJ(H) rearrangement.
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