Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.
Photo-CIDNP studies were performed on two protein fragments that both contain the double zinc-finger DNA-binding domain of the glucocorticoid receptor. In the absence of DNA, Tyr452 and Tyr474 are polarised in both fragments while Tyr497 is not. Addition of a palindromic glucocorticoid response element (GRE) results in the suppression of Tyr474 polarization while the polarization of Tyr452 is unaffected. The same result is observed upon adding a half GRE to the protein fragment indicating that the suppression of Tyr474 polarization is not due to protein-protein contacts but to interaction with DNA.
Kellenbach
E
E
Department of Chemistry, University of Utrecht, The Netherlands.
Härd
T
T
Boelens
R
R
Dahlman
K
K
Carlstedt-Duke
J
J
Gustafsson
J A
JA
van der Marel
G A
GA
van Boom
J H
JH
Maler
B
B
Yamamoto
K R
KR
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004396:Coloring Agents / Q000528:radiation effects; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010446:Peptide Fragments / Q000378:metabolism*; D010777:Photochemistry; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D012045:Regulatory Sequences, Nucleic Acid; D016335:Zinc Fingers
D004396:Coloring Agents; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D011965:Receptors, Glucocorticoid; D004247:DNA