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J. Biol. Chem., Vol. 266, Issue 24, 15832-15838, 08, 1991
MA Abril, M Buck and JL Ramos
Expression of the Pseudomonas putida TOL plasmid upper pathway operon
requires a promoter that belongs to the -12/-24 class. Stimulation of
transcription from this promoter is positively controlled by the
effector-activated XylR protein and requires a form of RNA-polymerase
holoenzyme containing the RpoN-encoded sigma factor, sigma 54. XylR-
dependent stimulation of transcription from the Pseudomonas TOL upper
pathway promoter was examined using deletions, insertions, and in vivo
dimethyl sulfate footprinting. Two upstream activator sequences were
identified in the -160 (UAS1) and -130 (UAS2) regions. Deletion of these
two regions abolished transcription activation, although conservation of
the UAS2 element alone allowed limited transcription stimulation.
Separation of UAS1 from UAS2 by half a turn or a full turn significantly
reduced XylR stimulation of transcription from the upper pathway operon
promoter. An inverted repeated ATTTGN2CAAAT (where N is any nucleoside),
which most likely represented the XylR recognition sequence, was
identified. Binding of XylR was observed in vivo in the absence of
effector, but changes in the binding pattern were induced in the presence
of m-methylbenzyl alcohol, a XylR effector. In vivo footprinting analysis
revealed that changes in the methylation pattern of G and T also occurred
in the -50 to -90 region, which is probably occupied by integration host
factor (IHF) protein. IHF was required for maximal expression from the TOL
upper pathway operon promoter in Escherichia coli. Separation of the IHF
site from UAS2 by a full helix turn did not significantly affect
stimulation of transcription, which is consistent with this region playing
a conformational role, rather than a regulatory one, in promoter function.
Activation of the Pseudomonas TOL plasmid upper pathway operon. Identification of binding sites for the positive regulator XylR and for integration host factor protein
Consejo Superior de Investigaciones Cientificas, Estacion Experimental del Zaidin, Department of Plant Biochemistry, Granada, Spain.
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