Osmolytes protect mitochondrial F0F1-ATPase complex against pressure inactivation

Saad-Nehme, Jorge; Silva, Jerson L.; Meyer‐Fernandes, José Roberto

doi:10.1016/s0167-4838(01)00137-6

Cited by 41 publications

(18 citation statements)

References 54 publications

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“…This might be due to the strengthening of hydrophobic interactions and enhanced formation of hydrogen bonds under high pressures leading to a more compact, rigid molecular structure reducing the thermal fluctuations caused by high temperatures (Balny & Masson, 1993;Gross & Jaenicke, 1994;Mozhaev, Lange, Kudryashova, & Balny, 1996;Boonyaratanakornkit, Park, & Clark, 2002). Protein unfolding at higher pressures occurs when water molecules penetrate into the protein interior causing the disruption of noncovalent intramolecular bonds (Nash & Jonas, 1997;Saad-Nehme, Silva, & Meyer-Fernandes, 2001). …”

Section: Combined Thermal and High Pressure Treatment Of Ppo In Applementioning

confidence: 99%

Inactivation kinetics of apple polyphenol oxidase in different pressure–temperature domains

Buckow¹,

Weiß²,

Knorr³

2009

Innovative Food Science & Emerging Technologies

142

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Section: Combined Thermal and High Pressure Treatment Of Ppo In Applementioning

confidence: 99%

Inactivation kinetics of apple polyphenol oxidase in different pressure–temperature domains

Buckow¹,

Weiß²,

Knorr³

2009

Innovative Food Science & Emerging Technologies

142

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“…The phosphorylation of ribose prevents leakage of the neutral sugar across the cell membrane. Carbohydrates have a baroprotective effect on bacteria and proteins [46][47][48], thus the ability for intracellular ribose accumulation may lead to a similar effect.…”

Section: Discussionmentioning

confidence: 99%

High pressure effects step-wise altered protein expression inLactobacillus sanfranciscensis

et al. 2002

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In this study we investigated the cellular response to the application of high hydrostatic pressure. High pressure is increasingly used for food preservation. With high resolution 2-D electrophoresis we compared the protein patterns of atmospherically grown Lactobacillus sanfranciscensis with those pressure treated up to 200 MPa. We performed the comparative study by using overlapping immobilized pH gradients covering the pH range from 2.5 up to 12 in order to maximize the resolution for the detection of stress relevant proteins. For improved quantitative analysis, staining with SyproRuby was used in addition to silver staining. By computer aided image analysis we detected more than a dozen spots within the pH range from 3.5 to 9 that were more than two-fold increased or 50% decreased in their intensity upon high pressure treatment. Two of them (approx. values: pI 4.0 and 4.2, respectively; M(r) approximately 15 000) have almost identical matrix-assisted laser desorption/ionization-time of flight mass spectrometry spectra and were identified by liquid chromatography-tandem mass spectrometry as putative homologs/paralogs to cold shock proteins of Lactococcus lactis. Their expression is opposed (i.e. the more acidic one is repressed, while the other one is induced); this effect is maximal at 1 h, 150 MPa. It was further remarkable that by monitoring the barosensitivity of the cells within 25 MPa steps, we observed a differential pressure induction or repression of the detected proteins as well. For example one protein (approx. values: pI 4.2, M(r) approximately 15 000) shows a maximum induction after 1 h, 150 MPa while another one (pI 7.5, M(r) approximately 25 000) is maximally induced after 1 h, 50/75 MPa. This indicates a successive cell response and different signalling pathways for these responses.

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“…In non-deep-sea studies, polyols were found to protect several proteins from pressure degradation (Athés et al, 1998;Ashie et al, 1999). Bovine mitochondrial ATPase complex was also protected by sugars, polyols, and betaine (Saad-Nehme et al, 2001). Some foodpoisoning microbes can survive pressure sterilization if they are provided with the methylamines betaine or carnitine, but not other osmolyte-type cosolutes (Smiddy et al, 2004).…”

Section: Extrinsic Adaptations To Pressure: Piezolytesmentioning

confidence: 99%

Co-evolution of proteins and solutions: protein adaptation versus cytoprotective micromolecules and their roles in marine organisms

Yancey

Siebenaller

2015

Journal of Experimental Biology

128

116

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Organisms experience a wide range of environmental factors such as temperature, salinity and hydrostatic pressure, which pose challenges to biochemical processes. Studies on adaptations to such factors have largely focused on macromolecules, especially intrinsic adaptations in protein structure and function. However, micromolecular cosolutes can act as cytoprotectants in the cellular milieu to affect biochemical function and they are now recognized as important extrinsic adaptations. These solutes, both inorganic and organic, have been best characterized as osmolytes, which accumulate to reduce osmotic water loss. Singly, and in combination, many cosolutes have properties beyond simple osmotic effects, e.g. altering the stability and function of proteins in the face of numerous stressors. A key example is the marine osmolyte trimethylamine oxide (TMAO), which appears to enhance water structure and is excluded from peptide backbones, favoring protein folding and stability and counteracting destabilizers like urea and temperature. Co-evolution of intrinsic and extrinsic adaptations is illustrated with high hydrostatic pressure in deep-living organisms. Cytosolic and membrane proteins and G-protein-coupled signal transduction in fishes under pressure show inhibited function and stability, while revealing a number of intrinsic adaptations in deep species. Yet, intrinsic adaptations are often incomplete, and those fishes accumulate TMAO linearly with depth, suggesting a role for TMAO as an extrinsic 'piezolyte' or pressure cosolute. Indeed, TMAO is able to counteract the inhibitory effects of pressure on the stability and function of many proteins. Other cosolutes are cytoprotective in other ways, such as via antioxidation. Such observations highlight the importance of considering the cellular milieu in biochemical and cellular adaptation.

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Osmolytes protect mitochondrial F0F1-ATPase complex against pressure inactivation

Cited by 41 publications

References 54 publications

Inactivation kinetics of apple polyphenol oxidase in different pressure–temperature domains

Inactivation kinetics of apple polyphenol oxidase in different pressure–temperature domains

High pressure effects step-wise altered protein expression inLactobacillus sanfranciscensis

Co-evolution of proteins and solutions: protein adaptation versus cytoprotective micromolecules and their roles in marine organisms

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