Characterization of BpH3, an H-NS-like protein in Bordetella pertussis.
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.
Goyard
S
S
Unité de Biochimie des Régulations Cellulaires, Institut Pasteur, Paris, France.
Bertin
P
P
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D001886:Bordetella pertussis / Q000737:chemistry*; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics*; D005786:Gene Expression Regulation; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
D001426:Bacterial Proteins; C107190:BpH3 protein, Bordetella pertussis; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria; D014157:Transcription Factors