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The tre operon of Bacillus subtilis is regulated at the transcriptional level by the Tre repressor (TreR) and by carbon catabolite repression. The molecular inducer of TreR is trehalose-6-phosphate, which is generated by transport of trehalose across the membrane by a specific Enzyme IITre (TreP) and simultaneous phosphorylation. It has been shown that TreP lacks the Enzyme IIA domain which is necessary for the phosphoryl transfer from phosphoenolpyruvate via Enzyme I and HPr. In this study, evidence is presented supporting the hypothesis of the involvement of the A domain from Enzyme IIGlc on trehalose utilization and its potential role in the regulation of the transcription of the tre operon.
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Michael K. Dahl (2006) studied this question.
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