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J Biol Chem, Vol. 274, Issue 41, 29358-29365, October 8, 1999
The Escherichia coli ssuEADCB Gene Cluster Is
Required for the Utilization of Sulfur from Aliphatic Sulfonates and Is
Regulated by the Transcriptional Activator Cbl
Jan R.
van der Ploeg ,
Roksana
Iwanicka-Nowicka§,
Tomasz
Bykowski§,
Monika M.
Hryniewicz§, and
Thomas
Leisinger
From the Institut für Mikrobiologie, Swiss
Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich,
Switzerland and § Institute of Biochemistry and Biophysics,
Polish Academy of Sciences, 02-106 Warsaw, Poland
The growth properties of an Escherichia
coli strain carrying a chromosomal deletion of the
ssuEADCB genes (formerly designated ycbPONME)
indicated that the products of this gene cluster are required for the
utilization of sulfur from aliphatic sulfonates. Sequence similarity
searches indicated that the proteins encoded by ssuA,
ssuB, and ssuC are likely to constitute an ABC
type transport system, whereas ssuD and ssuE
encode an FMNH2-dependent monooxygenase and an
NAD(P)H-dependent FMN reductase, respectively (Eichhorn, E., van der Ploeg, J. R., and Leisinger, T. (1999) J. Biol. Chem. 274, 26639-26646). Synthesis of -galactosidase from a
transcriptional chromosomal ssuE'-lacZ fusion
was repressed by sulfate or cystine and depended on the presence of a
functional cbl gene, which encodes a LysR-type
transcriptional regulator. Electrophoretic mobility shift assays with
the ssu promoter region and measurements of -galactosidase from plasmid-encoded ssuE'-'lacZ fusions
showed that full expression of the ssu operon required the
presence of a Cbl-binding site upstream of the 35 region. CysB, the
LysR transcriptional regulator for the cys genes, was not
required for expression of a chromosomal ssuE'-lacZ fusion
although the ssu promoter region contained three
CysB-binding sites. Integration host factor could also occupy three
binding sites in the ssu promoter region but had no
influence on expression of a chromosomal ssuE'-lacZ fusion.
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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