Pseudomonas Aeruginosa Contains an IHF-like Protein That Binds to the algD Promoter

Biochem Biophys Res Commun. 1993 Oct 15;196(1):416-421. doi: 10.1006/bbrc.1993.2265.

Abstract

An IHF-like protein has been purified from a Pseudomonas aeruginosa strain isolated from a cystic fibrosis patient, by the rapid purification method described for the isolation of IHF from Rhodobacter capsulatus. The IHF of P. aeruginosa is an alpha beta heterodimer (subunits of 10 and 11 kDa) similar to IHF from Escherichia coli and from R. capsulatus; the N-terminal amino acid sequences of the isolated subunits share a high degree of identity with their homologs from E. coli. P. aeruginosa IHF is able to bind to the promoter of the hydrogenase structural genes (hupSL) of R. capsulatus as do the other two IHF proteins. It is also demonstrated by gel retardation assays that P. aeruginosa IHF forms a stable complex with the algD promoter in vitro, an indication that the protein is involved in the regulation of algD gene expression in P. aeruginosa.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Carbohydrate Dehydrogenases / genetics*
  • DNA-Binding Proteins / metabolism*
  • Integration Host Factors
  • Molecular Sequence Data
  • Promoter Regions, Genetic / genetics*
  • Pseudomonas aeruginosa / genetics*
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Integration Host Factors
  • integration host factor, Pseudomonas
  • integration host factor, Rhodobacter
  • Carbohydrate Dehydrogenases
  • GDPmannose dehydrogenase