Regulatory effect of microbial alkyloxybenzenes of different structure on the stress response of yeast

Konanykhina, I. A.; Shanenko, E. F.; Лойко, Н. Г.; Nikolaev, Yu. A.; Эль-Регистан, Г. И.

doi:10.1134/s0003683808050116

Cited by 6 publications

(5 citation statements)

References 2 publications

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“…The effect of alkylhydroxybenzenes on the resistance of S. cerevisiae cells to heat shock and oxidative stress of lethal intensity depended on the hydrophobicity of the investigated compounds; C7-alkylhydroxybenzene at concentrations of 0.25-0.5 g/l caused a two-to fivefold increase in the resistance of yeast cells to hydrogen peroxide, whereas C12-alkylhydroxybenzene reduced it at all concentrations. C7-alkylhydroxybenzene and C12-alkylhydroxybenzene had a similar effect on yeast subjected to heat shock [81].…”

Section: Phenolic Lipids Affect Oxidation Processesmentioning

confidence: 67%

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Biological activity of phenolic lipids

Stasiuk

Kozubek

2009

Cell. Mol. Life Sci.

229

158

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Phenolic lipids are a very diversified group of compounds derived from mono and dihydroxyphenols, i.e., phenol, catechol, resorcinol, and hydroquinone. Due to their strong amphiphilic character, these compounds can incorporate into erythrocytes and liposomal membranes. In this review, the antioxidant, antigenotoxic, and cytostatic activities of resorcinolic and other phenolic lipids are described. The ability of these compounds to inhibit bacterial, fungal, protozoan and parasite growth seems to depend on their interaction with proteins and/or on their membrane-disturbing properties.

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Section: Phenolic Lipids Affect Oxidation Processesmentioning

confidence: 67%

“…A transition can result from the formation of micella-like nanostructures around DNA macromolecules by the interacting hexylresorcinol molecules [149]. A similar stabilizing effect was shown for Saccharomyces cerevisiae [81].…”

Section: Phenolic Lipids Inhibit Bacterial Fungal Protozoan and Pamentioning

confidence: 78%

Biological activity of phenolic lipids

Stasiuk

Kozubek

2009

Cell. Mol. Life Sci.

229

158

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“…For example, in the samples preincubated with C 12 and C 18 (Table 4). Such an effect of C 7 and C 9 AR may be ascribed to their adaptogenic and protective functions demonstrated previously [10,[21][22][23]. HSP synthesis induction factor F 2i and the residual number of CFU after heat shock of the cells pretreated with ARs were compared with the same values for non heated cells, taken as 100%, at each AR concentration; this revealed the adaptogenic function of long chain ARs (Table 4).…”

Section: Effect Of Alkylhydroxybenzenes On Luciferase Ther Mal Stabilmentioning

confidence: 54%

“…Studies of AR functions in generation of bacterial stress response demonstrated that various extreme factors (for example, heat shock) stimulated AR biosynthesis [21], while elevated AR levels affected cell stability [8,22,23] by means of increased func tional and operational stability of the enzymes [9,20,24] on the one hand, and activation of stress gene expression, on the other [10,13]. It was therefore log ical to assume that changes in AR concentration in a microbial culture can affect the induction of heat shock protein synthesis, in particular, syntesis of the IbpA chaperone [6].…”

Section: Effect Of Alkylhydroxybenzenes On Luciferase Ther Mal Stabilmentioning

confidence: 99%

“…Heat shock protein synthesis Produce no effect on HSP synthesis with im provement of cell resistance to heat stress Activate HSP synthesis with improvement of cell resistance to heat stress Inhibit HSP synthesis with decrease of cell re sistance to heat stress viously for bacteria and yeasts [10,[21][22][23] and pro vided for by the chemical chaperone properties of ARs [9,[17][18][19] and (2) their functional interference with the system of heat shock proteins [23]. As for the applied aspect of the obtained results, the nonspecific and multitargeted nature of AR binding to protein molecules provides for its reproduction not only in microbial, but also in heterologous living sys tems.…”

Section: Protein Denaturation Prevent Prevent Enhancementioning

confidence: 99%

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Effect of alkylresorcinols on thermal denaturation and refolding of bacterial luciferase and synthesis of heat shock proteins revealed in the luminescent molecular and cellular test systems

et al. 2014

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Molecular and cellular luminescent biotests were used to reveal the effects of five alkylresorcinol homologues (C 7 , C 9 , C 11 , C 12 , and C 18 AR) on the thermally induced denaturation and refolding of bac terial luciferases, as well as on the synthesis of heat shock proteins. The ARs activities were found to depend on their fine structure and concentration. The direct heat protective effect of short chain C 7 and C 9 AR on the chromatographically pure Photobactrium leiognathii luciferase/oxidoreductase was shown within a broad range of concentrations (10 -6 -10 -3 M). The long chain ARs homologues exhibited a similar heat protective effect at micromolar concentrations only, while their millimolar concentrations increased the sensitivity of the model proteins to thermal treatment. The recombinant strain Escherichia coli K12 MG1655, bearing con stitutively expressed Vibrio fischeri luxAB genes was used to investigate the ARs effect on the intracellular chaperone independent refolding of bacterial luciferase. The functional activity of heat inactivated enzyme was restored by micromolar concentrations of short chain ARs, while long chain homologues inhibited refolding over the wide concentration range. The recombinant luminescent E. coli strain bearing the induc ible ibpA'::luxCDABE genetic construction was used to determine the effect of ARs on the synthesis of heat shock proteins (HSP). The preincubation mode of bacterial cells with long chain alkylresorcinols led to the dose dependent stimulation of HSP synthesis (2.7 to 4 times), which confirmed that ARs function as "alar mones." Subsequent thermal treatment resulted in a 5 to 15 fold decrease of the following HSP induction compared to the control, while the number of viable cells opposite increased by 1.5 to 4 fold. Thus, pretreat ment of the bacterial cells with long chain ARs resulted in their preadaptation to subsequent thermally induced stress. Short chain ARs caused less pronounced HSP suppression, although this was still was accom panied by increased heat resistance of the AR pretreated bacterial cells.

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