Rhen M, Väisänen-Rhen V, Saraste M, Korhonen T K
Gene. 1986;49(3):351-60. doi: 10.1016/0378-1119(86)90371-9.
The organization of genes encoding the blood group M-specific hemagglutinin (M-agglutinin) of Escherichia coli strain IH11165 was studied with a cloned 6.5-kb DNA segment. This DNA segment contains at least five genes which code for the polypeptides of 12.5, 30, 80, 18.5 and 21 kDa. The 30-, 80- and 21-kDa polypeptides are synthesized as precursors that are approximately 2 kDa larger. The 21-kDa polypeptide was identified as the M-agglutinin subunit by its reactivity with anti-M-agglutinin serum. Nucleotide sequence analysis of the corresponding gene showed that the M-agglutinin precursor had a 24-amino acid (aa) signal sequence, while the mature protein is 146 aa residues long. Although the organization of the M-agglutinin gene cluster resembles those of other E. coli adhesins, there is no significant sequence homology between the M-agglutinin subunit and the subunits of the other potentially related proteins in E. coli.
利用一个克隆的6.5kb DNA片段,对编码大肠杆菌IH11165血型M特异性血凝素(M-凝集素)的基因组织进行了研究。该DNA片段至少包含五个基因,它们编码12.5、30、80、18.5和21kDa的多肽。30kDa、80kDa和21kDa的多肽以前体形式合成,前体比成熟多肽大约大2kDa。通过与抗M-凝集素血清的反应,鉴定出21kDa的多肽为M-凝集素亚基。对相应基因的核苷酸序列分析表明,M-凝集素前体有一个24个氨基酸(aa)的信号序列,而成熟蛋白长146个aa残基。虽然M-凝集素基因簇的组织与其他大肠杆菌粘附素的相似,但M-凝集素亚基与大肠杆菌中其他潜在相关蛋白的亚基之间没有明显的序列同源性。