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Metal Oxyanion Stabilization of the Rat Glucocorticoid Receptor Is Independent of Thiols. by K J Modarress; A H Cavanaugh; P K Chakraborti; S S Simons is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The ability of sodium molybdate, both to stabilize the steroid binding activity of glucocorticoid receptors and to prevent the activation of receptor-steroid complexes to a DNA binding species, has long been thought to involve thiols. Two receptor thiols in particular, Cys-656 and Cys-661 of rat receptors, have been suspected. The requirements for the action of molybdate, as well as two other metal oxyanions (tungstate and vanadate) known to exert the same effects as molybdate, have now been examined with receptors in which these thiols, or a third cysteine in the steroid binding cavity (Cys-640), have been mutated to serine. No mutation prevented any metal oxyanion from either stabilizing steroid-free receptors or blocking the activation of complexes for binding to nonspecific or specific DNA sequences. Thus, Cys-640, Cys-656, and Cys-661 are not required for any of the effects of molybdate, tungstate, or vanadate with rat glucocorticoid receptors. Studies with hybrid receptors, and with a 16-kDa steroid binding core fragment containing only 3 cysteines at positions 640, 656, and 661, indicated that no cysteine of the rat receptor was needed to maintain responsiveness to molybdate

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Author

K J Modarress; A H Cavanaugh; P K Chakraborti; S S Simons

Publisher

Elsevier BV

Published

1994

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)