Parales J, Greenberg E P
Department of Microbiology, University of Iowa, Iowa City, 52242.
J Bacteriol. 1991 Feb;173(3):1357-9. doi: 10.1128/jb.173.3.1357-1359.1991.
The amino-terminal sequences and amino acid compositions of the three major and two minor polypeptides constituting the filaments of Spirochaeta aurantia periplasmic flagella were determined. The amino-terminal sequence of the major 37.5-kDa outer layer polypeptide is identical to the sequence downstream of the proposed signal peptide of the protein encoded by the S. aurantia flaA gene. However, the amino acid composition of the 37.5-kDa polypeptide is not in agreement with that inferred from the sequence of flaA. The 34- and 31.5-kDa major filament core polypeptides and the 33- and 32-kDa minor core polypeptides show a striking similarity to each other, and the amino-terminal sequences of these core polypeptides show extensive identity with homologous proteins from members of other genera of spirochetes. An additional 36-kDa minor polypeptide that occurs occasionally in preparations of S. aurantia periplasmic flagella appears to be mixed with the 37.5-kDa outer layer polypeptide or a degradation product of this polypeptide.
测定了构成橙色螺旋体周质鞭毛丝的三种主要和两种次要多肽的氨基末端序列和氨基酸组成。主要的37.5 kDa外层多肽的氨基末端序列与橙色螺旋体flaA基因编码蛋白的假定信号肽下游的序列相同。然而，37.5 kDa多肽的氨基酸组成与从flaA序列推断的不一致。34 kDa和31.5 kDa的主要丝核心多肽以及33 kDa和32 kDa的次要核心多肽彼此之间表现出惊人的相似性，并且这些核心多肽的氨基末端序列与来自其他螺旋体属成员的同源蛋白具有广泛的同一性。在橙色螺旋体周质鞭毛制剂中偶尔出现的另一种36 kDa次要多肽似乎与37.5 kDa外层多肽或该多肽的降解产物混合在一起。
