Abstract
A. Keynan (Israel Institute of Biological Research, Ness Ziona, Israel), Z. Evenchik, H. O. Halvorson, and J. W. Hastings. Studies on the activation of bacterial endospores. J. Bacteriol. 88:313–318. 1964.—Heat activation of bacterial endospores was imitated by suspending spores in reducing agents (mercaptoethanol or thioglycolate) or in a pH less than 4.5. Urea (6 m) had no effect on spores. In addition to the well-known activation at 65 C for 45 min, spores were also activated by exposure to 34 C for 48 hr. The activation by heat and by reducing agents was reversible; the reverse reaction was temperature-dependent. No reversion occurred at −20 C, whereas at 28 C the spores reversed to their original dormant state within 72 hr.
It is suggested that the heat-activation phenomenon could be explained by assuming that heat or reducing agents change the tertiary structure of a protein responsible for the maintenance of the dormant state by reducing the disulfide linkages which stabilize the protein in a specific configuration. The partial denaturation of this protein is reversible by reoxidation of the reduced disulfide bonds.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
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