A biochemist discovers new RNA polymerase activity in crude extracts of cells derived from an exotic fungus. The RNA polymerase initiates transcription only from a single, highly specialized promoter. As she purifies the polymerase, its activity declines, and the purified enzyme is completely inactive unless she adds crude extract to the reaction mixture. What could explain these observations? Contamination by small interfering RNAs (siRNAs) during purification could decrease RNA polymerase activity. The Lac repressor bound to the lac operon could block RNA polymerase activity. Proteolysis of the RNA polymerase could be responsible for loss of enzyme activity. Dissociation of factors needed for activity, such as a specificity factor, could decrease RNA polymerase activity. The purification buffers could cause the RNA polymerase to be unstable, thus decreasing enzyme activity.

Human Anatomy & Physiology (11th Edition)
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ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
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A biochemist discovers new RNA polymerase activity in crude extracts of cells derived from an exotic fungus. The RNA
polymerase initiates transcription only from a single, highly specialized promoter. As she purifies the polymerase, its activity
declines, and the purified enzyme is completely inactive unless she adds crude extract to the reaction mixture.
What could explain these observations?
Contamination by small interfering RNAs (siRNAs) during purification could decrease RNA polymerase activity.
The Lac repressor bound to the lac operon could block RNA polymerase activity.
Proteolysis of the RNA polymerase could be responsible for loss of enzyme activity.
Dissociation of factors needed for activity, such as a specificity factor, could decrease RNA polymerase activity.
The purification buffers could cause the RNA polymerase to be unstable, thus decreasing enzyme activity.
Transcribed Image Text:A biochemist discovers new RNA polymerase activity in crude extracts of cells derived from an exotic fungus. The RNA polymerase initiates transcription only from a single, highly specialized promoter. As she purifies the polymerase, its activity declines, and the purified enzyme is completely inactive unless she adds crude extract to the reaction mixture. What could explain these observations? Contamination by small interfering RNAs (siRNAs) during purification could decrease RNA polymerase activity. The Lac repressor bound to the lac operon could block RNA polymerase activity. Proteolysis of the RNA polymerase could be responsible for loss of enzyme activity. Dissociation of factors needed for activity, such as a specificity factor, could decrease RNA polymerase activity. The purification buffers could cause the RNA polymerase to be unstable, thus decreasing enzyme activity.
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