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J. Biol. Chem., Vol. 269, Issue 28, 18371-18377, 07, 1994
Z Li and B Demple
A genetic response of Escherichia coli to nitric oxide or to superoxide-
generating agents such as paraquat is controlled by the soxRS locus. The
intracellular redox signals generated by these agents are sensed by the
SoxR protein which, when activated, functions as a potent activator of soxS
transcription. The resulting increased level of SoxS protein then activates
approximately 10 genes that constitute the soxRS regulon. Although the SoxS
protein is homologous to the COOH-terminal region of the AraC family of
regulatory proteins, the mechanism by which SoxS protein activates the
soxRS regulon promoters is unknown. We identified in extracts of cells
expressing high levels of SoxS protein a DNA binding activity specific for
fragments containing soxRS- regulated promoters. This binding activity was
purified to physical homogeneity and proved to be the SoxS protein, as
confirmed by NH2- terminal amino acid sequencing. The purified SoxS protein
bound specifically to the promoters of the micF, zwf, nfo, and sodA genes.
Multiple DNA-protein complexes were formed by SoxS in a concentration-
dependent fashion with each of these promoters. This binding of SoxS
protein also facilitated the subsequent binding of E. coli RNA polymerase
to both the micF and the nfo promoters. The binding sites of SoxS in the
zwf and micF promoters were identified by DNase I footprinting, which
revealed an extended protected region immediately upstream of the
respective -35 sites. These results indicate that the small SoxS protein
(M(r) of only 12,900) is a direct transcriptional activator of the
oxidative stress genes of the soxRS regulon, although the possible
involvement of other proteins in transcription activation by SoxS has not
been ruled out.
SoxS, an activator of superoxide stress genes in Escherichia coli. Purification and interaction with DNA
Department of Molecular and Cellular Toxicology, Harvard School of Public Health, Boston, Massachusetts 02115.
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