Characterization of FapR, a positive regulator of expression of the 987P operon in enterotoxigenic Escherichia coli.

Abstract:

:Expression of the 987P gene cluster is activated by the adjacent IS1 element of an STpa transposon. Nucleotide sequence analysis of the 987P-DNA region contiguous with this IS1 element revealed the presence of an open reading frame designated fapR, encoding a basic protein of 260 amino acid residues with a molecular mass of 30,349 Daltons. The gene product, FapR, possesses similarity to a number of positive regulators of gene expression: VirF, Rns, AppY and EnvY. Moreover, a 43-amino-acid residue sequence in the C-terminal part of FapR is similar to the C-terminal domain of AraC, RhaR, and RhaS. Expression of fapR is dependent on the adjacent IS1 element. The FapR protein appears to be required for activation of the silent promoter of the fimbrial subunit gene, fapC.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Klaasen P,de Graaf FK

doi

10.1111/j.1365-2958.1990.tb00556.x

subject

Has Abstract

pub_date

1990-10-01 00:00:00

pages

1779-83

issue

10

eissn

0950-382X

issn

1365-2958

journal_volume

4

pub_type

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