Inactivation of the FNR protein of Escherichia coli by targeted mutagenesis in the N-terminal region.
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.
Spiro
S
S
Department of Microbiology, University of Sheffield, UK.
Guest
J R
JR
D000595:Amino Acid Sequence; D000693:Anaerobiosis; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D003545:Cysteine; D004252:DNA Mutational Analysis; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D003545:Cysteine