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Regulation of hemolysin synthesis in escherichia coli determined by hly genes of human origin


, : Regulation of hemolysin synthesis in escherichia coli determined by hly genes of human origin. Molecular & General Genetics 199(1): 111-116

The secretion of a 107K polypeptide into the medium from a hemolytic E. coli K12 strain was previously reported. In addition, it was demonstrated that hemolysin production was correlated with the presence of this polypeptide in the growth medium in a large number of E. coli isolates of human and animal origin. It was confirmed that the 107K polypeptide was indeed hemolysin; both hemolytic activty and the 107K polypeptide show a similar pattern of accumulation during the growth cycle; identical levels were produced in 3 different growth media; they have the same half-life in minimal medium. The results also show that the expression of hemolysin is not influenced by the growth medium or subject to catabolite repression. Expression was apparently switched off as cells enter the later exponential phase of growth. The previously reported variation in hemolysin production in different media is entirely due to the instability of the hemolysin itself. Degradation of the 107K polypeptide in the medium was accompanied by the accumulation of a major breakdown product of 60K.

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Related references

Nicaud, J.M.; Mackman, N.; Gray, L.; Holland, I.B., 1985: Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin. We have previously reported the secretion of a 107K polypeptide into the medium from a haemolytic E. coli K12 strain (Mackman and Holland 1984a). In addition, we demonstrated that haemolysin production was correlated with the presence of this poly...

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