Premium
Identification of a fatty acyl responsive regulator (FarR) in Escherichia coli
Author(s) -
Quail Michael A.,
Dempsey Clare E.,
Guest John R.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01264-4
Subject(s) - biochemistry , escherichia coli , gene cluster , fatty acid , gene , biology , chemistry , microbiology and biotechnology
FarR (formerly P30) has been identified as a fatty acid and fatty acyl‐CoA responsive DNA‐binding protein. It is encoded by the farR gene ( g30 ) in the citric acid cycle gene cluster of E. coli ( gltA‐sdhCDAB‐sucABCD‐farR ). The amplified FarR protein specifically bound to the farR promoter ( P farR ) and exhibited weak binding to the citrate synthase and lipoamide dehydrogenase promoters. Binding at P farR was abolished by long‐chain fatty acids and their CoA thioesters. In DNaseI footprints, FarR binding at P faR protected two sites each characterised by two related 10‐bp direct repeats. It is suggested that farR autoregulates farR expression and may modulate citric acid cycle expression in response to long‐chain fatty acids.