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J Biol Chem, Vol. 273, Issue 5, 2645-2652, January 30, 1998
From the Laboratory of Bacterial Pathogenesis and Immunology, The
Rockefeller University, New York, New York 10021
The expression of many virulence determinants in
Staphylococcus aureus is controlled by regulatory loci such
as agr and sar. We have previously shown that
the SarA protein is required for optimal transcription of RNAII and
RNAIII in the agr locus. To define the specific molecular
interaction, we overexpressed SarA as a glutathione
S-transferase (GST) fusion protein by cloning the 372-base
pair (bp) sarA gene into the vector. The purified GST-SarA
as well as cleaved SarA were able to bind specifically to the P2, P3,
and the combined P2-P3 promoter fragments of agr in gel
shift assays. Using monoclonal antibodies to SarA, we found that SarA
is a part of the retarded protein-DNA complex as evidenced by the
formation of a supershifted band. The SarA binding site on the
agr promoter, mapped by DNase I footprinting assay, covered a 29-bp region between the P2 and P3 promoters devoid of any direct repeats. A synthetic 45-bp fragment encompassing the 29-bp sequence also bound the SarA protein in band shift assays. Serial in-frame deletion analysis of sarA revealed that, with the exception
of 15 residues in the N terminus, almost all of SarA (residues 16-124) is essential for agr binding activity. Northern analysis
confirmed that only the sar mutant clone containing a
truncated sarA gene with a 15-residue deletion in the N
terminus (SarA16-124) could activate agr
transcription to a level approaching that of the full-length
counterpart (SarA1-124). Taken together, these data
indicated that SarA is a DNA-binding protein with binding specificity
to the P2 and P3 interpromoter region of agr, thereby activating RNAII and RNAIII transcription.
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