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Characterization of FapR, a positive regulator of expression of the 987P operon in enterotoxigenic Escherichia Coli
Author(s) -
Klaasen P.,
Graaf F. K.
Publication year - 1990
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.1365-2958.1990.tb00556.x
Subject(s) - biology , operon , enterotoxigenic escherichia coli , escherichia coli , regulator , microbiology and biotechnology , genetics , gene , enterotoxin
Summary Expression of the 987P gene cluster is activated by the adjacent IS 1 element of an ST pa transposon. Nucleotide sequence analysis of the 987P‐DNA region contiguous with this IS 1 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 30349 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 IS 1 element. The FapR protein appears to be required for activation of the silent promoter of the fimbrial subunit gene, fapC