In the absence of glucocorticoid hormone, the glucocorticoid hormone receptor pr
ID: 58200 • Letter: I
Question
In the absence of glucocorticoid hormone, the glucocorticoid hormone receptor protein is found
E.in an inactive form in the plasma membrane
When methionine is abundant, S-adenosyl methionine allosterically regulates synthesis of methionine in bacteria by
A.in the cytosol, bound to an inactivating protein B.in an inactive form in the nucleus that has bound a specific DNA sequence, but cannot bind to other activators to trigger gene expression C.in an inactive form bound to Mediator in the nucleus D.in an inactive form in the nucleus that is unable to bind DNAE.in an inactive form in the plasma membrane
When methionine is abundant, S-adenosyl methionine allosterically regulates synthesis of methionine in bacteria by
A.binding to the Met repressor, causing a change in conformation so that the repressor binds DNA and blocks expression of the genes encoding the enzymes that synthesize methionine B.binding to the Met repressor, causing a change in conformation so that the repressor binds DNA and increases the level of expression of the genes encoding the enzymes that synthesize methionine C.binding to the Met repressor, causing a change in conformation so that the repressor is inhibited from binding to DNA D.binding to a regulatory site on the first enzyme in the pathway for methionine synthesis, causing a change in conformation that inhibits the enzyme activity, and thus decreases methionine synthesis E.binding to a regulatory site on the first enzyme in the pathway for methionine synthesis, causing a change in conformation that activates the enzyme activity, and thus increases methionine synthesisExplanation / Answer
(A) In the absence of glucocorticoid hormone, the glucocorticoid hormone receptor protein is found in the cytosol, bound to an inactivating protein. It binds to certain proteins such as heat shock proteins
(D) When methionine is abundant, S-adenosyl methionine allosterically regulates synthesis of methionine in bacteria by binding to a regulatory site on the first enzyme in the pathway for methionine synthesis, causing a change in conformation that inhibits the enzyme activity, and thus decreases methionine synthesis
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