Identification of a DNA binding protein that recognizes the nonamer recombinational signal sequence of immunoglobulin genes.

B. D. Halligan, Stephen Desiderio

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)7019-7023
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number20
StatePublished - Oct 1987

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Immunoglobulin Genes
DNA-Binding Proteins
Protein Sorting Signals
DNA
Lymphocytes
Light
Ion Exchange Chromatography
Base Pairing
Genes
Carrier Proteins
Binding Sites
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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AB - 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.

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