Fur (ferric uptake regulation) protein interaction with target DNA: comparison of gel retardation, footprinting and electron microscopy analyses.
Fur-DNA interactions were analyzed within the regulatory regions of aerobactin and hemolysin operons by a combination of biochemical and ultrastructural methods. Cartography of the Fur binding sites, carried out from electron micrographs, agreed with the data obtained by DNase I footprinting. Visualization of the complexes confirmed the specificity and metal-dependence of Fur binding and demonstrated that the protein polymerizes on its binding sites. Such a polymerization could be involved in the repression process of the bacterial regulator.
Fréchon
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Laboratoire d'Ecologie Microbienne, URA 147 du CNRS, Institut Gustave-Roussy, Villejuif, France.
Le Cam
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D001426:Bacterial Proteins / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D004926:Escherichia coli / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D006459:Hemolysin Factors / Q000235:genetics*; D006877:Hydroxamic Acids; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009876:Operon; D011401:Promoter Regions, Genetic; D012333:RNA, Messenger / Q000235:genetics; D012097:Repressor Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D006877:Hydroxamic Acids; D012333:RNA, Messenger; D012097:Repressor Proteins; C068477:ferric uptake regulating proteins, bacterial; C031819:aerobactin; D004247:DNA