Characterization of BpH3, an H-NS-like protein in Bordetella pertussis

Molecular Microbiology
S Goyard, P Bertin

Abstract

This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of beta-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria.

Citations

Nov 11, 2003·Trends in Microbiology·Christian Tendeng, Philippe N Bertin
Sep 5, 2001·The EMBO Journal·X LiH L Mobley
Apr 13, 2013·Nucleic Acids Research·Yuanyuan QuJie Yan
Sep 9, 2008·Journal of Bacteriology·Blair R G GordonJun Liu
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Jul 18, 2020·Journal of Proteome Research·Jakub NovakPeter Sebo

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