Abstract
Azotobacter vinelandii ferredoxin I (AvFdI) is one member of a class of 7Fe ferredoxins found in a variety of organisms that are all capable of aerobic growth. Disruption of the fdxA gene, which encodes AvFdI, leads to overexpression of its redox partner, NADPH-ferredoxin reductase (FPR). In this study the mechanism of FdI-mediated regulation of FPR was investigated. Northern analysis has shown that regulation is at the level of fpr transcription, the start site for transcription has been identified, and it is preceded by a canonical sigma 70-type bacterial promoter. Gel mobility shift assays show that there is a putative regulatory protein in A. vinelandii that binds specifically upstream of the -35 region. That protein is not AvFdI. A palindromic sequence was identified as a putative binding site, and randomization of that sequence completely eliminates binding of the putative regulatory protein. A luciferase reporter gene was placed under control of the A. vinelandii fpr promoter and introduced into wild type and FdI- strains of A. vinelandii. Luciferase activity was enhanced 7-fold in the FdI- mutant relative to the wild type. Alteration of the palindromic sequence reduced the luciferase levels in the FdI- strain to those o...Continue Reading
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