Hairpin coding end opening is mediated by RAG1 and RAG2 proteins

Eva Besmer, Jorge Mansilla-Soto, Sylvanie Cassard, Dennis J. Sawchuk, Greg Brown, Moshe Sadofsky, Susanna M. Lewis, Michel C. Nussenzweig, Patricia Cortes

Research output: Contribution to journalArticle

110 Scopus citations

Abstract

Despite the importance of hairpin opening in antigen receptor gene assembly, the molecular machinery that mediates this reaction has not been defined. Here, we show that RAG1 plus RAG2 can open DNA hairpins. Hairpin opening by RAGs is not sequence specific, but in Mg2+, hairpin opening occurs only in the context of a regulated cleavage complex. The chemical mechanism of harpin opening by RAGs resembles RSS cleavage and 3′ end processing by HIV integrase and Mu transposase in that these reactions can proceed through alcoholysis. Mutations in either RAG1 or RAG2 that interfere with RSS cleavage also interfere with hairpin opening, suggesting that RAGs have a single active site that catalyzes several distinct DNA cleavage reactions.

Original languageEnglish (US)
Pages (from-to)817-828
Number of pages12
JournalMolecular Cell
Volume2
Issue number6
DOIs
StatePublished - Dec 1998
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Besmer, E., Mansilla-Soto, J., Cassard, S., Sawchuk, D. J., Brown, G., Sadofsky, M., Lewis, S. M., Nussenzweig, M. C., & Cortes, P. (1998). Hairpin coding end opening is mediated by RAG1 and RAG2 proteins. Molecular Cell, 2(6), 817-828. https://doi.org/10.1016/S1097-2765(00)80296-8