Sakamoto Y, Sutherland K J, Tamaoka J, Kobayashi T, Kudo T, Horikoshi K
The RIKEN Institute, Saitama, Japan.
J Gen Microbiol. 1992 Oct;138(10):2159-66. doi: 10.1099/00221287-138-10-2159.
Motility of the alkalophilic Bacillus sp. C-125, a flagellate bacterium, was demonstrated to be Na(+)- and pH-dependent. Flagellin protein from this strain was purified to homogeneity and the N-terminal sequence determined. Using the hag gene of Bacillus subtilis as a probe, the hag gene of Bacillus sp. C-125 was identified and cloned into Escherichia coli. Sequencing of this hag gene revealed that it encodes a protein of 272 amino acids (M(r) 29,995). The predicted N terminal sequence of this protein was identical to that determined by N-terminal sequencing of the flagellin protein from strain C-125. The alkalophilic Bacillus sp. C-125 flagellin shares homology with other known flagellins in both the N- and C-terminal regions. The middle portion, however, shows considerable differences, even from that of flagellin from the related species, B. subtilis.
嗜碱芽孢杆菌C-125是一种具鞭毛的细菌,其运动性被证明依赖于Na⁺和pH。该菌株的鞭毛蛋白被纯化至同质,并测定了其N端序列。以枯草芽孢杆菌的hag基因为探针,鉴定出嗜碱芽孢杆菌C-125的hag基因,并将其克隆到大肠杆菌中。对该hag基因的测序表明,它编码一种含272个氨基酸(分子量29,995)的蛋白质。该蛋白质预测的N端序列与通过对C-125菌株鞭毛蛋白进行N端测序所确定的序列相同。嗜碱芽孢杆菌C-125的鞭毛蛋白在N端和C端区域与其他已知鞭毛蛋白具有同源性。然而中部区域,即使与相关物种枯草芽孢杆菌的鞭毛蛋白相比,也显示出相当大的差异。