Open AccessIdentification of murine nuclear proteins that bind to the conserved octamer sequence of the immunoglobulin promoter region.
Author(s) -
J H Hanke,
Nicholas F. Landolfi,
Philip W. Tucker,
J D Capra
Publication year - 1988
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.85.10.3560
Subject(s) - histone octamer , nuclear protein , biology , microbiology and biotechnology , dna binding protein , gene , dna , immunoglobulin gene , antibody , biochemistry , genetics , transcription factor , histone , nucleosome
Sequence-specific DNA-affinity chromatography was used to purify a nuclear protein from the B-cell leukemia cell line BCL1 that specifically binds to the octamer sequence ATTTGCAT, previously shown to be important in the regulation of immunoglobulin genes. This protein has a molecular mass of approximately 70 kDa and is responsible for the protein-DNA interaction specific to lymphoid cells. Other proteins of molecular mass 80-90 kDa and 50-55 kDa that specifically bind to the octamer sequence were also identified. These results demonstrate that the octamer is recognized by several biochemically distinct nuclear proteins, perhaps to differentially regulate the expression of immunoglobulin genes.