Cloning and characterization of a protein binding to the J kappa recombination signal sequence of immunoglobulin genes.
A protein with molecular weight of 60,000 that binds to the recombination signal sequence (RS) of the immunoglobulin J kappa segment was purified from the nuclear extract of a murine pre B cell line 38B9. This binding protein was found in lymphoid cell lines but not in non-lymphoid cell lines. The Kd value of the J kappa RS binding protein to the J kappa RS was 1 nM. The cDNA clone (RBP-2) was isolated based on partial amino-acid sequence of this protein. This cDNA encodes 526 amino-acid residues, and its sequence does not show extensive overall homology with any known proteins, but displays an interesting homology to a 40-residue region that is conserved among a subset of site specific recombinase (integrase family).
Hamaguchi
Y
Y
Department of Medical Chemistry, Kyoto University Faculty of Medicine, Japan.
Mastunami
N
N
Yamamoto
Y
Y
Kuze
K
K
Kangawa
K
K
Matsuo
H
H
Kawaichi
M
M
Honjo
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000302:isolation & purification; D005803:Genes, Immunoglobulin; D051379:Mice; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000235:genetics; D011995:Recombination, Genetic; D015183:Restriction Mapping
D004268:DNA-Binding Proteins; D021382:Protein Sorting Signals; D004247:DNA