Analysis of glucocorticoid receptor subspecies binding to DNA-cellulose and isolated nuclei.
Conversion of the glucocorticoid receptor into a DNA-binding protein results in the generation of several distinct receptor subspecies (peaks A-E) which can be resolved by anion exchange chromatography. In vitro, the fraction of the receptor population (approx. 40%) which gains a capacity to bind DNA-cellulose is preferentially transformed into the peak A species by a process that was enhanced by the presence of KCl. At 0.4 M KCl, virtually all of the DNA-binding receptor was in the peak A form. Isolated nuclei also exhibit a receptor binding profile similar to that observed with DNA-cellulose.
Gruol
D J
DJ
Regulatory Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037.
Wolfe
K A
KA
Safarian
S
S
D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D002482:Cellulose / Q000031:analogs & derivatives / Q000378:metabolism; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D008223:Lymphoma; D051379:Mice; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification / Q000378:metabolism*; D014222:Triamcinolone Acetonide / Q000378:metabolism
D004268:DNA-Binding Proteins; C033190:DNA-cellulose; D011965:Receptors, Glucocorticoid; D002482:Cellulose; D004247:DNA; D014222:Triamcinolone Acetonide