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Inactivation of the FNR protein of Escherichia coli by targeted mutagenesis in the N ‐terminal region
Author(s) -
Spiro S.,
Guest J. R.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00080.x
Subject(s) - cysteine , biology , escherichia coli , residue (chemistry) , mutagenesis , site directed mutagenesis , biochemistry , gene , function (biology) , mutation , genetics , enzyme , mutant
Summary The FNR protein of Escherichia coli is a regulatory protein that activates the transcription of its target genes in response to oxygen limitation. Site‐directed mutagenesis was used to show that a 28‐residue N ‐terminal segment containing three cysteines is essential for normal FNR function. The cysteine residue which is centrally located in the three‐cysteine cluster (Cys‐Ala‐Ile‐His‐Cys‐Gln‐Asp‐Cys) was also shown to be essential for FNR activity. Possible mechanisms by which this cysteine residue might function in the response of FNR to anaerobiosis are discussed.