Abstract:
:The ndh gene of Escherichia coli which encodes an NADH dehydrogenase contains a putative FNR-binding site in its upstream non-coding region, and its expression has been investigated using an ndh-lacZ fusion. Expression of the fusion was found to be reduced during anaerobic growth, and experiments with hosts containing an fnr mutation and/or a multicopy fnr+ plasmid indicated that the anaerobic repression of the ndh gene is mediated by the FNR protein. Thus FNR can function as an anaerobic repressor as well as an anaerobic transcriptional activator. The results are consistent with the FNR-binding function attributed to the proposed consensus sequence. Using frdA- and ndh-lacZ fusions exhibiting positive and negative regulation by FNR, it was further shown that the depletion of metal ions in growth media with chelating agents mimics oxygen with respect to the activity of FNR. Possible roles for metal ions in the oxygen-sensing pathway associated with FNR function are discussed.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Spiro S,Roberts RE,Guest JRdoi
10.1111/j.1365-2958.1989.tb00207.xsubject
Has Abstractpub_date
1989-05-01 00:00:00pages
601-8issue
5eissn
0950-382Xissn
1365-2958journal_volume
3pub_type
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