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The structural and functional organization of H‐NS‐like proteins is evolutionarily conserved in Gram‐negative bacteria
Author(s) -
Bertin Philippe,
Benhabiles Nora,
Krin Evelyne,
LaurentWinter Christine,
Tendeng Christian,
Turlin Evelyne,
Thomas Annick,
Danchin Antoine,
Brasseur Robert
Publication year - 1999
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1999.01176.x
Subject(s) - biology , rhodobacter , escherichia coli , complementation , peptide sequence , bacteria , hypothetical protein , in silico , genetics , conserved sequence , fusion protein , rhodobacter sphaeroides , gene , biochemistry , recombinant dna , mutant
The structural gene of the H‐NS protein, a global regulator of bacterial metabolism, has been identified in the group of enterobacteria as well as in closely related bacteria, such as Erwinia chrysanthemi and Haemophilus influenzae . Isolated outside these groups, the BpH3 protein of Bordetella pertussis exhibits a low amino acid conservation with H‐NS, particularly in the N‐terminal domain. To obtain information on the structure, function and/or evolution of H‐NS, we searched for other H‐NS‐related proteins in the latest databases. We found that HvrA, a trans ‐activator protein in Rhodobacter capsulatus , has a low but significant similarity with H‐NS and H‐NS‐like proteins. This Gram‐negative bacterium is phylogenetically distant from Escherichia coli . Using theoretical analysis (e.g. secondary structure prediction and DNA binding domain modelling) of the amino acid sequence of H‐NS, StpA (an H‐NS‐like protein in E. coli ), BpH3 and HvrA and by in vivo and in vitro experiments (e.g. complementation of various H‐NS‐related phenotypes and competitive gel shift assay), we present evidence that these proteins belong to the same class of DNA binding proteins. In silico analysis suggests that this family also includes SPB in R. sphaeroides , XrvA in Xanthomonas oryzae and VicH in Vibrio cholerae . These results demonstrate that proteins structurally and functionally related to H‐NS are widespread in Gram‐negative bacteria.