In vitro interaction of the IHF-like proteins Acinetobacter junii and Proteus vulgaris with ihf sites

Abstract

The ability of the IHF-like proteins of Acinetobacter junii and Proteus vulgaris to interact with the H′ attP and p R′ ihf sites of λ DNA was investigated. IHF from A. junii and P. vulgaris was found to bind the examined ihf sites in a way similar to IHF from Escherichia coli as shown by gel mobility shift DNA binding assays and footprinting analysis. The three IHF proteins bound to the p R′ ihf site that overlaps the −35 region of that promoter and in vitro repression of transcription by each IHF was observed. These results confirm that IHF-like proteins from Gram-negative bacteria can recognize the same specific DNA sequences and appear to be important in regulation of transcription.