Alm R A, Stroeher U H, Manning P A
Department of Microbiology and Immunology, University of Adelaide, South Australia.
Mol Microbiol. 1988 Jul;2(4):481-8. doi: 10.1111/j.1365-2958.1988.tb00054.x.
The EI T or haemolysin, product of hlyA, is exported from Vibrio cholerae as a Mr 80,000 protein which can be subsequently cleaved to give two proteins of Mr 65,000 and 15,000. Nucleotide sequence analysis has demonstrated that hlyA encodes a protein of Mr 82,250 with a potential 18-amino-acid signal sequence. The non-haemolytic classical strain 569B has been shown to have a structural gene defect rather than a defect in secretion. By non-reciprocal recombination it was possible to transfer this defect onto a plasmid and show that a truncated hlyA product of Mr 27,000 is made in Escherichia coli K-12 minicells. Nucleotide sequence analysis demonstrates an 11-base-pair deletion which would result in a Mr 26,940 protein probably loosely associated with the membrane.
由hlyA基因产物产生的EI T或溶血素以分子量为80,000的蛋白质形式从霍乱弧菌中输出,随后可被切割成分子量为65,000和15,000的两种蛋白质。核苷酸序列分析表明,hlyA编码一种分子量为82,250的蛋白质,带有一个潜在的18个氨基酸的信号序列。非溶血型经典菌株569B已被证明存在结构基因缺陷而非分泌缺陷。通过非相互重组,有可能将这种缺陷转移到质粒上,并表明在大肠杆菌K-12微小细胞中产生了一种分子量为27,000的截短hlyA产物。核苷酸序列分析显示有一个11个碱基对的缺失,这将导致一种可能与膜松散结合的分子量为26,940的蛋白质。