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The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2.

V(D)J recombination is initiated by the specific binding of the RAG1-RAG2 (RAG1/2) complex to the heptamer-nonamer recombination signal sequences (RSS). Several steps of the V(D)J recombination reaction can be reconstituted in vitro with only RAG1/2 plus the high-mobility-group protein HMG1 or HMG2. Here we show that the RAG1 homeodomain directly interacts with both HMG boxes of HMG1 and HMG2 (HMG1,2). This interaction facilitates the binding of RAG1/2 to the RSS, mainly by promoting high-affinity binding to the nonamer motif. Using circular-permutation assays, we found that the RAG1/2 complex bends the RSS DNA between the heptamer and nonamer motifs. HMG1,2 significantly enhance the binding and bending of the 23RSS but are not essential for the formation of a bent DNA intermediate on the 12RSS. A transient increase of HMG1,2 concentration in transfected cells increases the production of the final V(D)J recombinants in vivo.

Pubmed ID: 10490593

Authors

  • Aidinis V
  • Bonaldi T
  • Beltrame M
  • Santagata S
  • Bianchi ME
  • Spanopoulou E

Journal

Molecular and cellular biology

Publication Data

October 3, 1999

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI40191

Mesh Terms

  • Binding Sites
  • DNA-Binding Proteins
  • High Mobility Group Proteins
  • Homeodomain Proteins
  • Nucleic Acid Conformation
  • Protein Binding
  • Receptors, Antigen
  • Recombination, Genetic