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J Biol Chem, Vol. 274, Issue 8, 4754-4763, February 19, 1999
The Bacillus stearothermophilus Mannitol
Regulator, MtlR, of the Phosphotransferase System
A DNA-BINDING PROTEIN, REGULATED BY HPr AND
IICBmtl-DEPENDENT PHOSPHORYLATION
Sytse A.
Henstra,
Menno
Tuinhof,
Ria H.
Duurkens, and
George T.
Robillard
From the Departments of Biochemistry, the Groningen Biomolecular
Sciences and Biotechnology Institute, University of Groningen,
Nijenborgh 4, 9747 AG Groningen, The Netherlands
D-Mannitol is taken up by
Bacillus stearothermophilus and phosphorylated via a
phosphoenolpyruvate-dependent phosphotransferase system
(PTS). The genes involved in the mannitol uptake were recently cloned
and sequenced. One of the genes codes for a putative transcriptional regulator, MtlR. The presence of a DNA binding helix-turn-helix motif
and two antiterminator-like PTS regulation domains, suggest that MtlR
is a DNA-binding protein, the activity of which can be regulated by
phosphorylation by components of the PTS. To demonstrate DNA binding of
MtlR to a region upstream of the mannitol promoter, by DNA
footprinting, MtlR was overproduced and purified. EI, HPr, IIAmtl, and IICBmtl of B. stearothermophilus were purified and used to demonstrate that
MtlR can be phosphorylated and regulated by HPr and
IICBmtl, in vitro. Phosphorylation of MtlR by
HPr increases the affinity of MtlR for its binding site, whereas
phosphorylation by IICBmtl results in a reduction of this
affinity. The differential effect of phosphorylation, by two different
proteins, on the DNA binding properties of a bacterial transcriptional
regulator has not, to our knowledge, been described before. Regulation
of MtlR by two components of the PTS is an example of an elegant
control system sensing both the presence of mannitol and the need to
utilize this substrate.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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