Stabilization of enzymes by dormancy autoinducers as a possible mechanism of resistance of resting microbial forms |
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Authors: | A. I. Kolpakov O. N. Il’inskaya M. M. Bespalov F. G. KupriyanovaAshina V. F. Gal’chenko B. I. Kurganov G. I. El’-Registan |
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Affiliation: | (1) Institute of Microbiology, Russian Academy of Sciences, pr. 60-letiya Oktyabrya 7, k. 2, 117811 Moscow, Russia;(2) Kazan State University, ul. Kremlevskaya 18, 420008 Kazan, Russia;(3) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskiipr. 33, 117071 Moscow, Russia |
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Abstract: | Alkyl-substituted hydroxybenzenes (AHBs), autoinducers of microbial dormancy (ord 1 factors), were found to stabilize the structure of protein macromolecules, making them metabolically less active and more resistant to stresses. In vitro experiments with theBacillus intermedius ribonuclease and chymotrypsin showed that the degree of the physical and chemical stability of these enzymes treated with AHBs depends on their concentration and incubation time. Experiments with RNase, which is capable of refolding, i.e., renaturation after heat denaturation, revealed that AHBs efficiently interact with both intact and denatured proteins. The data obtained allow the inference to be made thatd 1 factors may play the role of natural chemical chaperons, blocking metabolism in dormant cells through the formation of catalytically inactive thermostable complexes with enzymes. |
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Keywords: | dormancy dormancy autoinducers metabolic block thermostability of enzymes d1 factors of microorganisms chemical chaperons alkyl-substituted hydroxybenzenes |
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