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Identification of high-specificity H-NS binding site in LEE5 promoter of enteropathogenic Esherichia coli (EPEC)

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Abstract

Histone-like nucleoid structuring protein (H-NS) is a small but abundant protein present in enteric bacteria and is involved in compaction of the DNA and regulation of the transcription. Recent reports have suggested that H-NS binds to a specific AT rich DNA sequence than to intrinsically curved DNA in sequence independent manner. We detected two high-specificity H-NS binding sites in LEE5 promoter of EPEC centered at -110 and -138, which were close to the proposed consensus H-NS binding motif. To identify H-NS binding sequence in LEE5 promoter, we took a random mutagenesis approach and found the mutations at around -138 were specifically defective in the regulation by H-NS. It was concluded that H-NS exertsmaximumrepression via the specific sequence at around -138 and subsequently contacts a subunit of RNAP through oligomerization.

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Correspondence to Hyon E. Choy.

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Bhat, A.P., Shin, M. & Choy, H.E. Identification of high-specificity H-NS binding site in LEE5 promoter of enteropathogenic Esherichia coli (EPEC). J Microbiol. 52, 626–629 (2014). https://doi.org/10.1007/s12275-014-3562-x

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  • DOI: https://doi.org/10.1007/s12275-014-3562-x

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