S. Goyard, IDENTIFICATION AND CHARACTERIZATION OF BPH2, A NOVEL HISTONE H1 HOMOLOG IN BORDETELLA-PERTUSSIS, Journal of bacteriology, 178(11), 1996, pp. 3066-3071
A basic protein, BpH2, with an apparent molecular mass of 18 kDa was p
urified from Bordetella pertussis, and the corresponding gene, bph2, w
as cloned. Sequence analysis revealed some homology to the H1 class of
eukaryotic histones and to AlgP protein of Pseudomonas aeruginosa. Bp
H2 binds both single- and double-stranded DNA in a nonspecific manner,
Deletion of the corresponding gene in B. pertussis generated a BpH2 n
ull mutant with an altered growth rate in which the expression of two
virulence factors, adenylate cyclase-hemolysin (CyaA) and filamentous
hemagglutinin (FhaB), was reduced. It is suggested that BpH2 may exhib
it specific regulatory functions through its interaction with chromoso
mal DNA.