Characterization of a novel DNA binding domain within the amino-terminal region of the RAG-1 protein

Biochem Mol Biol Int. 1998 Jul;45(3):535-44. doi: 10.1080/15216549800202922.

Abstract

Rag-1 and Rag-2 are the critical components of the V-(D)-J recombinase required for site-specific recombination of the antigen receptor genes. In this study, we have examined the ability of recombinant (r) Rag-1 and Rag-2 to bind the recombination signal sequences (RSS) and have determined that rRag-1, but not rRag-2, is able to directly bind DNA. rRAG-1 DNA binding activity was found to reside within a novel amino-terminal arginine-rich (RR) domain with partial homology to a variety of nucleic acid binding domains. Although the RR-domain did not demonstrate RSS-specificity, this DNA binding domain may stabilize the interaction of RAG-1 with, or increase the affinity for, the V-(D)-J recombination signals.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Homeodomain Proteins / chemistry*
  • Homeodomain Proteins / metabolism
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins
  • Protein Conformation
  • RNA-Binding Proteins / chemistry
  • Recombinant Proteins / chemistry
  • Sequence Deletion
  • Sequence Homology, Amino Acid

Substances

  • DNA-Binding Proteins
  • Homeodomain Proteins
  • Nuclear Proteins
  • RAG2 protein, human
  • RNA-Binding Proteins
  • Recombinant Proteins
  • V(D)J recombination activating protein 2
  • RAG-1 protein
  • DNA