Metabolite gene regulation of the L-arabinose operon in Escherichia coli with indoleacetic acid and other indole derivatives.
نویسندگان
چکیده
The ability of indole derivatives to facilitate RNA polymerase transcription of the L-arabinose operon in Escherichia coli was shown to require the catabolite activator protein (CAP) as well as the araC gene product. Adenosine 3',5'-monophosphate (cAMP) was not obligatory for araBAD transcription when the cells were grown in the presence of 1 mM indole-3-acetic acid or in the presence of indole-3-acetamide, indole-3-propionic acid, indole-3-butyric acid, or 5-hydroxyindole-3-acetic acid. However, these indole derivatives were unable to circumvent the cAMP requirement for the induction of the lactose and the maltose operons. Catabolic repression occurred when glucose was added to cells grown in the presence of L-arabinose and 1 mM indoleacetic acid or 1 mM cAMP. This effect was reversed at higher concentrations of indoleacetic acid or cAMP. The induction and the catabolite repression phenomena were quantitated by measuring the differential rate of synthesis of L-arabinose isomerase (the araA gene product). These results indicated that indole metabolites from various living systems may regulate gene expression and may be involved in "metabolite gene regulation."
منابع مشابه
Deoxyribonucleic acid-ribonucleic acid hybridization studies on the L-Arabinose operon of Escherichia coli B-r.
An increase in the rate of synthesis of ara-specific messenger ribonucleic acid as measured by deoxyribonucleic acid-ribonucleic acid hybridization has been detected in the induced wild-type (ara(+)) strain of Escherichia coli B/r as compared with the uninduced control, thus providing evidence that regulation of the positively controlled l-arabinose operon is at the level of transcription.
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 77 4 شماره
صفحات -
تاریخ انتشار 1980