Goyard S
Unité de Biochimie des Régulations Cellulaires, Institut Pasteur, Paris, France.
J Bacteriol. 1996 Jun;178(11):3066-71. doi: 10.1128/jb.178.11.3066-3071.1996.
A basic protein, BpH2, with an apparent molecular mass of 18 kDa was purified from Bordetella pertussis, and the corresponding gene, bph2, was cloned. Sequence analysis revealed some homology to the H1 class of eukaryotic histones and to AlgP protein of Pseudomonas aeruginosa. BpH2 binds both single- and double-stranded DNA in a nonspecific manner. Deletion of the corresponding gene in B. pertussis generated a BpH2 null 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 exhibit specific regulatory functions through its interaction with chromosomal DNA.
从百日咳博德特氏菌中纯化出一种表观分子量为18 kDa的碱性蛋白BpH2,并克隆了相应的基因bph2。序列分析显示,它与真核生物组蛋白H1类以及铜绿假单胞菌的AlgP蛋白有一定的同源性。BpH2以非特异性方式结合单链和双链DNA。在百日咳博德特氏菌中缺失相应基因产生了一个BpH2缺失突变体,其生长速率发生改变,两种毒力因子腺苷酸环化酶溶血素(CyaA)和丝状血凝素(FhaB)的表达降低。提示BpH2可能通过与染色体DNA相互作用发挥特定的调节功能。