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Active domains in wild‐type and mutant glucocorticoid receptors.

[3H]Triamcinolone acetonide was used to tag covalently specific glucocorticoid receptors by photoaffinity labelling at lambda greater than or equal to 320 nm. Receptors of wild‐type mouse lymphoma cells and two glucocorticoid resistant mutants of “nuclear transfer deficient” (nt‐) and “increased nuclear transfer” (nti) phenotypes, respectively, were used. Wild‐type and nt‐ receptors yielded radiolabelled polypeptide bands of mol. wt. 98 000 as revealed by gel electrophoresis under denaturing conditions and fluorography. In contrast, the nti receptor had a mol. wt. of 42 000. Partial proteolysis of the wild‐type receptor with alpha‐chymotrypsin resulted in a fragment of mol. wt. 39 000 which still contained the steroid binding site but had increased affinity for DNA indistinguishable from that of the nti receptor. Chymotrypsin thus removed a domain from the wild‐type receptor polypeptide which is involved in modulating DNA binding. The same domain is missing from the nti receptor.