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(Received for publication, December 17, 1996, and in revised form, February 20, 1997)
From the Department of Biology, University of Konstanz,
78434 Konstanz, Germany
The pathway of trehalose utilization in
Escherichia coli is different at low and high osmolarity.
The low osmolarity system takes up trehalose as trehalose 6-phosphate
which is hydrolyzed to glucose and glucose 6-phosphate.
treB and treC, the genes for the enzymes
involved, form an operon that is controlled by TreR (encoded by
treR), the repressor of the system, for which trehalose 6-phosphate is the inducer. We have cloned and sequenced
treR. The protein contains 315 amino acids with a molecular
weight of 34,508. TreR was purified and shown to bind as a dimer
trehalose 6-phosphate and trehalose with a Kd of 10 and 280 µM, respectively. The conformations of the
protein differ from each other with either one or the other
substrate-bound. Protease treatment removed the DNA-binding domain from
the intact protein leaving the dimerization domain (a 29-kDa
carboxyl-terminal fragment) intact. Nuclease protection experiments
revealed a palindromic sequence located directly upstream of the
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13026-13032
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
35
promoter sequence of treB that functions as the operator of
the system.
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