Open AccessComplex protein binding within the mouse immunoglobulin heavy-chain enhancer.
Author(s) -
Craig L. Peterson,
Kathryn Calame
Publication year - 1987
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.7.12.4194
Subject(s) - enhancer , footprinting , biology , immunoglobulin heavy chain , nuclease , deoxyribonuclease i , microbiology and biotechnology , binding site , dna binding protein , plasma protein binding , biochemistry , dna , transcription factor , gene , base sequence
We have begun to purify and characterize several proteins which bind to the mouse immunoglobulin heavy-chain enhancer to understand the molecular interactions important for enhancer activity. Three proteins which bind to different sites on the immunoglobulin heavy-chain enhancer have been chromatographically separated and partially purified. One protein binds a site which has not been reported previously and does not bind to other reported protein-binding sites on the immunoglobulin heavy-chain enhancer. Binding-site boundaries for the three partially purified proteins have been precisely mapped by methylation interference, DNase I footprinting, and orthophenanthroline/copper chemical nuclease footprinting. We have also characterized these three proteins with respect to dissociation rate constants.