Inactivation of the FNR protein of Escherichia coli by targeted mutagenesis in the N-terminal region.

Abstract:

: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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Spiro S,Guest JR

doi

10.1111/j.1365-2958.1988.tb00080.x

subject

Has Abstract

pub_date

1988-11-01 00:00:00

pages

701-7

issue

6

eissn

0950-382X

issn

1365-2958

journal_volume

2

pub_type

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