In vitro interactions of the histone-like protein IHF with the algD promoter, a critical site for control of mucoidy in Pseudomonas aeruginosa

C. D. Mohr, V. Deretic

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The ability of the histone-like element Integration Host Factor (IHF) to interact with the algD promoter was investigated. IHF from Escherichia coli was found to bind to the algD promoter and to form multiple protein-DNA complexes in gel mobility shift DNA binding assay. The highest affinity binding site for IHF was mapped by DNaseI footprinting analysis. This site spanned nucleotides -50 to -85 relative to the algD mRNA start site and overlapped a sequence matching the IHF consensus sequence WATCAANNNNTTR in 12 out of 13 base pairs. Previous studies have shown that deletion of sequences including a portion of this site adversely affects algD promoter activity. IHF binding to the algD promoter induced DNA bending. Western blot analysis with antibodies against E. coli IHF detected a cross-reactive protein of a similar molecular mass in Pseudomonas aeruginosa, suggesting the presence of an analogous factor in this organism.

Original languageEnglish (US)
Pages (from-to)837-844
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume189
Issue number2
DOIs
StatePublished - Dec 15 1992

Bibliographical note

Funding Information:
We thank H.A. Nash, A.E. Granston, and D. Deretic for the gifts of proteins and sera. This work was supported by grant AI31139 from the National Institutes of Health and grant G229 from the Cystic Fibrosis Foundation. C.D.M. was supported in art by trainin grant T32 AIO7272-06 from the National Institutes of Health an B by Predoctora Traineeship grant 5405 from the Cystic Fibrosis Foundation.

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