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J. Biol. Chem., Vol. 275, Issue 32, 24709-24714, August 11, 2000
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From the Department of Microbial Biotechnology, Centro Nacional de
Biotecnología CSIC, Campus de Cantoblanco,
28049 Madrid, Spain
Production of the siderophore aerobactin in
Escherichia coli is transcriptionally metalloregulated
through the iron-dependent binding of the Fur
(ferric uptake regulator) to a
large region (>100 base pairs) within the cognate promoter in
the pColV-K30 plasmid. We show in this article that such an unusually
long operator results from the specific addition of degenerate repeats
5'-NAT(A/T)AT-3' and not from a fortuitous occupation of the DNA
adjacent to the primary binding sites by an excess of the repressor.
Furthermore, the protection pattern revealed by DNase I and hydroxyl
radical footprinting reflected a side-by-side oligomerization of the
protein along an extended DNA stretch. This type of DNA-protein
interactions is more like those observed in some eukaryotic factors and
nucleoid-associated proteins than typical of specific prokaryotic regulators.
Evidence of an Unusually Long Operator for the Fur Repressor
in the Aerobactin Promoter of Escherichia coli*
,
*
This work was supported by Contracts BIO4-CT97-2040 and
QLRT-1999-00041 of the European Union and by Grant BIO98-0808 of
the Comisiòn Interministerial de Ciencia y Tecnología.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a Fellowship of Fundación Ramón Areces.
Present address: Inst. für Genetik. Biozentrum, Weinbergweg, 22 06120 Halle (Saale) Germany.
§
To whom correspondence should be addressed: Dept. of Microbial
Biotechnology, Centro Nacional de Biotecnología-CSIC, Campus de
Cantoblanco, 28049 Madrid, Spain. Tel.: 34-91-585-4536; Fax: 34-91-585-4506; E-mail: vdlorenzo@cnb.uam.es.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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