PMID:9148912
| Citation |
Horlacher, R and Boos, W (1997) Characterization of TreR, the major regulator of the Escherichia coli trehalose system. J. Biol. Chem. 272:13026-32 |
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| Abstract |
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 microM, 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 -35 promoter sequence of treB that functions as the operator of the system. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Cloning, Molecular; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes, Bacterial; Genes, Regulator; Molecular Sequence Data; Repressor Proteins/genetics; Sequence Alignment; Trehalose/genetics |
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