ORBi: Bertin P. - The Structural And Functional Organization Of H-Ns-Like Proteins Is Evolutionarily Conserved In Gram-Negative Bacteria

Reference : The Structural And Functional Organization Of H-Ns-Like Proteins Is Evolutionarily Conse...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/63687

Title :	The Structural And Functional Organization Of H-Ns-Like Proteins Is Evolutionarily Conserved In Gram-Negative Bacteria
Language :	English
Author, co-author :	Bertin, P. [> > > >]
	Benhabiles, N. [> > > >]
	Krin, E. [> > > >]
	Laurent-Winter, C. [> > > >]
	Tendeng, C. [> > > >]
	Turlin, E. [> > > >]
	Thomas, Annick [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
	Danchin, A. [> > > >]
	Brasseur, Robert [Université de Liège > > Gembloux Agro-Bio Tech >]
Publication date :	1999
Journal title :	Molecular Microbiology
Volume :	31
Issue/season :	1
Pages :	319-29
ISSN :	0950-382X
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.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/63687

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