Article
Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon

https://doi.org/10.1016/0022-2836(90)90284-SGet rights and content

Abstract

The levanase gene (sacC) of Bacillus subtilis is the distal gene of a fructose-inducible operon containing five genes. The complete nucleotide sequence of this operon was determined. The first four genes levD, levE, levF and levG encode polypeptides that are similar to proteins of the mannose phosphotransferase system of Escherichia coli. The levD and levE gene products are homologous to the N and C-terminal part of the enzyme IIIMan, respectively, whereas the levF and levG gene products have similarities with the enzymes IIMan. Surprisingly, the polypeptides encoded by the levD, levE, levF and levG genes are not involved in mannose uptake, but form a fructose phosphotransferase system in B. subtilis. This transport is dependent on the enzyme I of the phosphotransferase system (PTS) and is abolished by deletion of levF or levG and by mutations in either levD or levE. Four regulatory mutations (sacL) leading to constitutive expression of the levanase operon were mapped using recombination experiments. Three of them were characterized at the molecular level and were located within levD and levE. The levD and levE gene products that form part of a fructose uptake PTS act as negative regulators of the operon. These two gene products may be involved in a PTS-mediated phosphorylation of a regulator, as in the bgl operon of E. coli.

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      The best-studied activator is LevR of B. subtilis (P23914), which controls the expression of the levDEFG operon encoding the Lev-PTS (IIA, IIB, IIC, IIDLev; P26379-81). The Lev-PTS shares 46% amino acid sequence identity with the E. coli Man-PTS [100,101]. It transports fructose, which is released when the fructose polymer levane is degraded by an exofructosidase (levanase).

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    This work was supported by grants from the Pasteur Institute, the Centre National de la Recherche Scientifique and the Fondation pour la Recherche Médicale.

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