Hydroxybutyrate prevents protein aggregation in the halotolerant bacterium <Emphasis Type="Italic">Pseudomonas</Emphasis> sp. CT13 under abiotic stress |
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Authors: | Gabriela Soto Lorena Setten Christian Lisi Camila Maurelis Matteo Mozzicafreddo Massimiliano Cuccioloni Mauro Angeletti Nicolás Daniel Ayub |
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Institution: | 1.Instituto de Genética Ewald A. Favret (CICVyA-INTA),Castelar,Argentina;2.Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET),C1033AAJ Ciudad Autónoma de Buenos Aires,Argentina;3.Cátedra de Farmacobotánica, Facultad de Ciencias, Exactas, Químicas y Naturales,Universidad de Morón,Morón,Argentina;4.School of Biosciences and Biotechnology,University of Camerino,Camerino,Italy |
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Abstract: | Polyhydroxybutyrate (PHB), a typical carbon and energy storage compound, is widely found in Bacteria and Archae domains. This
polymer is produced in response to conditions of physiological stress. PHB is composed of repeating units of β-hydroxybutyrate
(R-3HB). It has been previously shown that R-3HB functions as an osmolyte in extremophile strains. In this study, Pseudomonas sp. CT13, a halotolerant bacterium, and its PHB synthase-minus mutant (phaC) were used to analyze the chaperone role of R-3HB. The production of this compound was found to be essential to salt stress
resistance and positively correlated with salt concentration, suggesting that PHB monomer acts as a compatible solute in Pseudomonas sp. CT13. R-3HB accumulation was also associated with the prevention of protein aggregation under combined salt and thermal
stresses in Pseudomonas sp. CT13. Physiological concentrations of R-3HB efficiently reduced citrate synthase (CS) aggregation and stabilized the
enzymatic activities of CS during thermal stress. Docking analysis of the CS/R-3HB interaction predicted the stability of
this complex under physiological concentrations of R-3HB. Thus, in vivo, in vitro and in silico analyses suggest that R-3HB
can act as a chemical chaperone. |
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