
Identification of a DNA binding protein that recognizes the nonamer recombinational signal sequence of immunoglobulin genes.
Author(s) -
Brian D. Halligan,
Stephen Desiderio
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.20.7019
Subject(s) - dna , immunoglobulin light chain , gene , microbiology and biotechnology , recombination signal sequences , immunoglobulin gene , dna binding protein , biology , base pair , dna sequencing , genetics , antibody , transcription factor , recombination , recombination activating gene
Extracts of nuclei from B- and T-lymphoid cells contain a protein that binds specifically to the conserved nonamer DNA sequence within the recombinational signals of immunoglobulin genes. Complexes with DNA fragments from four kappa light-chain joining (J) segments have the same electrophoretic mobility. Nonamer-containing DNA fragments from heavy-chain and light-chain genes compete for binding. Within the 5'-flanking DNA of the J kappa 4 gene segment, the binding site has been localized to a 27-base-pair interval spanning the nonamer region. The binding activity is recovered as a single peak after ion-exchange chromatography. The site of binding of the protein and its presence in nuclei of lymphoid cells suggest that it may function in the assembly of immunoglobulin genes.