TY - JOUR
T1 - Protein-protein interactions between the DNA-binding domains of nuclear receptors
T2 - Influence on DNA-binding
AU - Dahlman-Wright, Karin
AU - Grandien, Kaj
AU - Nilsson, Stefan
AU - Gustafsson, Jan Åke
AU - Carlstedt-Duke, Jan
N1 - Funding Information:
and Marika R6nnholm for generously providing the ~t-GR DBD monoclonal antibodies and Dr Anthony Wright for critical reading of the manuscript. This project was supported by grants from the Swedish Medical Research Council (2819) and the Swedish National Board for Technical Development. J.C.-D. is the recipient of a Swedish Medical Council Fellowship.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1993/4
Y1 - 1993/4
N2 - The glucocorticoid and thyroid hormone receptors have the capacity to bind as dimers to palindromic DNA-binding sites. Protein-protein interactions between the DNA-binding domains of glucocorticoid receptor dimers restrict the DNA-binding to elements where the half-sites are separated by three base pairs, whereas DNA-binding by the thyroid hormone receptor does not appear to require a strict half-site spacing. We have previously shown that a five amino-acid segment close the the C-terminal zinc-binding site (D-box) was involved in dimerization of the glucocorticoid receptor (GR) DNA-binding domain (Dahlman-Wright et al., 1991, J. Biol. Chem., 266, 3107-3112). Here we provide functional evidence, using mutated thyroid hormone receptor DNA-binding domains, that this five amino acid segment (D-box) of the GR interacts with the equivalent segment on the second DNA-binding domain in the dimer. In contrast, the thyroid hormone receptor DNA-binding domain binds to palindromic thyroid hormone response elements in a weakly co-operative manner, independent of the D-box.
AB - The glucocorticoid and thyroid hormone receptors have the capacity to bind as dimers to palindromic DNA-binding sites. Protein-protein interactions between the DNA-binding domains of glucocorticoid receptor dimers restrict the DNA-binding to elements where the half-sites are separated by three base pairs, whereas DNA-binding by the thyroid hormone receptor does not appear to require a strict half-site spacing. We have previously shown that a five amino-acid segment close the the C-terminal zinc-binding site (D-box) was involved in dimerization of the glucocorticoid receptor (GR) DNA-binding domain (Dahlman-Wright et al., 1991, J. Biol. Chem., 266, 3107-3112). Here we provide functional evidence, using mutated thyroid hormone receptor DNA-binding domains, that this five amino acid segment (D-box) of the GR interacts with the equivalent segment on the second DNA-binding domain in the dimer. In contrast, the thyroid hormone receptor DNA-binding domain binds to palindromic thyroid hormone response elements in a weakly co-operative manner, independent of the D-box.
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U2 - 10.1016/0960-0760(93)90338-W
DO - 10.1016/0960-0760(93)90338-W
M3 - Article
C2 - 8499333
AN - SCOPUS:0027315947
VL - 45
SP - 239
EP - 250
JO - Journal of Steroid Biochemistry and Molecular Biology
JF - Journal of Steroid Biochemistry and Molecular Biology
SN - 0960-0760
IS - 4
ER -