Abstract :
[en] 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.
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