The role of alterations in membrane lipid composition in enabling physiological adaptation of organisms to their physical environment

Hazel, Jeffrey R.; Williams, Emma

doi:10.1016/0163-7827(90)90002-3

Cited by 902 publications

(661 citation statements)

References 322 publications

Supporting

Mentioning

626

Contrasting

Unclassified

Order By: Relevance

“…At present, it is difficult to answer. It has been reported that the activities of many membraneassociated enzymes decrease under high pressure, 14) but the enzymes used in those studies were obtained from non-piezophiles. Many of the enzyme activities of nonpiezophiles are known to be inhibited under high pressure even if the enzymes are soluble, although comparable enzymes from piezophiles are pressure tolerant.…”

mentioning

confidence: 99%

Piezotolerance of the Respiratory Terminal Oxidase Activity of the PiezophilicShewanella violaceaDSS12 as Compared with Non-PiezophilicShewanellaSpecies

Tamegai

Ota

Haga

et al. 2011

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

The facultative piezophile Shewanella violacea DSS12 is known to alter its respiratory components under the influence of hydrostatic pressure during growth, suggesting that it has a respiratory system that functions in adaptation to high pressure. We investigated the pressure-and temperature-dependencies of the respiratory terminal oxidase activity of the membrane of S. violacea relative to non-piezophilic Shewanella species. We observed that the activity in the membrane of S. violacea was more resistant to high pressure than those of non-piezophilic Shewanella even though DSS12 was cultured under atmospheric pressure. On the other hand, the temperature dependency of this activity was almost the same for all of the tested strain regardless of optimal growth temperature. Both high pressure and low temperature are expected to lower protein flexibility, causing a decrease in enzyme activity, but the results of this study suggest that the mechanism maintaining enzyme activity under high hydrostatic pressure is different from that at low temperature. Additionally, the responses of the activity to the pressure-and temperature-changes were independent of membrane lipid composition. Therefore, the piezotolerance of the respiratory terminal oxidases of S. violacea is perhaps dependent on the properties of the protein itself and not on the lipid composition of the membrane. Our observations suggest that S. violacea constitutively express piezotolerant respiratory terminal oxidases that serve adaptation to the deep-sea environment.

show abstract

mentioning

confidence: 99%

Piezotolerance of the Respiratory Terminal Oxidase Activity of the PiezophilicShewanella violaceaDSS12 as Compared with Non-PiezophilicShewanellaSpecies

Tamegai

Ota

Haga

et al. 2011

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

show abstract

“…Many GPCRs are known to form dimers, and this structural conformation is critical to proper function (Bulenger et al, 2005;Comar et al, 2014;Morita, 2010;Swezey and Somero, 1982). Additionally, proteins that form oligomeric assemblies are highly susceptible to functional changes at even modest pressures (Hazel and Williams, 1990;Morita, 2010). The dimer interface for most GPCRs, including cephalopod and bovine rhodopsins, has been reported to lie on the outer face of helices IV and V (Bockaert and Pin, 1999;Bulenger et al, 2005;Fotiadis et al, 2003;Liang et al, 2003) where the residues that we have identified as being under selection in both fish and cephalopod opsins are located.…”

Section: Evolution Of Protein Compressibilitymentioning

confidence: 79%

“…An extrinsic change common to many deep-sea animals is that of homeoviscous adaptation to maintain membrane fluidity (Behan et al, 1992;Eguchi et al, 1994;Hazel and Williams, 1990;Somero, 1992). Another is the use of trimethylamine oxide (TMAO) to stabilize proteins (Yancey et al, 2014;Siebenaller, 1999, 2015).…”

Section: Introductionmentioning

confidence: 99%

Evolution under pressure and the adaptation of visual pigment compressibility in deep-sea environments

Porter

Roberts

Partridge

2016

Molecular Phylogenetics and Evolution

View full text Add to dashboard Cite

Understanding the link between how proteins function in animals that live in extreme environments and selection on specific properties of amino acids has proved extremely challenging. Here we present the discovery of how the compressibility of opsin proteins in two evolutionarily distinct animal groups, teleosts and cephalopods, appears to be adapted to the high-pressure environment of the deep-sea. We report how in both groups, opsins in deeper living species are calculated to be less compressible. This is largely due to a common set of amino acid sites (bovRH#159, 196, 213, 275) undergoing positive destabilizing selection in six of the twelve amino acid physiochemical properties that determine protein compressibility. This suggests a common evolutionary mechanism to reduce the adiabatic compressibility of opsin proteins. Intriguingly, the sites under selection are on the proteins' outer faces at locations known to be involved in opsin-opsin dimer interactions.

show abstract

“…The temperatureindependence of these changes suggested that temperature is not the sole trigger for desaturase induction. One alternative possible determinant is oxygen, which acts as the terminal electron acceptor for aerobic desaturations [16]. Moreover, oxygen had been suggested to influence fatty acid desaturase activity significantly in nitrogen-purged plant tissue preparations [17].…”

Section: Scheme 1 Diagrammatic Representation Of the Nv6 Desaturase Smentioning

confidence: 99%

Oxygen induction of a novel fatty acid n−6 desaturase in the soil protozoon, Acanthamoeba castellanii

Rutter

Thomas

Herbert

et al. 2002

Biochemical Journal

View full text Add to dashboard Cite

Induction of fatty acid desaturation is very important for the temperature adaptation of poikilotherms. However, in oxygen-limited late-exponential-phase Acanthamoebacastellanii cultures, oxygen alone was able to induce increased activity of a fatty acid desaturase that converts oleate into linoleate and which has been implicated in the temperature adaptation of this organism. Experiments with Δ10-nonadecenoate showed that the enzyme is an n-6 desaturase rather than a Δ12-desaturase. It also used preferentially 1-acyl-2-oleoyl-phosphatidylcholine as substrate and NAD(P)H as electron donor. The involvement of cytochrome b5 as an intermediate electron carrier was shown by difference spectra measurements and anti-(cytochrome b5) antibody experiments. Of the three protein components of the desaturase complex, oxygen only increased the activity of the terminal (cyanide-sensitive) protein during n-6 desaturase induction. The induction of this terminal protein paralleled well the increase in overall oleate n-6 desaturation. The ability of oxygen to induce oleate desaturase independently of temperature in this lower eukaryotic animal model is of novel intrinsic interest, as well as being important for the design of future experiments to determine the molecular mechanism of temperature adaptation in poikilotherms.

show abstract

The role of alterations in membrane lipid composition in enabling physiological adaptation of organisms to their physical environment

Cited by 902 publications

References 322 publications

Piezotolerance of the Respiratory Terminal Oxidase Activity of the PiezophilicShewanella violaceaDSS12 as Compared with Non-PiezophilicShewanellaSpecies

Piezotolerance of the Respiratory Terminal Oxidase Activity of the PiezophilicShewanella violaceaDSS12 as Compared with Non-PiezophilicShewanellaSpecies

Evolution under pressure and the adaptation of visual pigment compressibility in deep-sea environments

Oxygen induction of a novel fatty acid n−6 desaturase in the soil protozoon, Acanthamoeba castellanii

Contact Info

Product

Resources

About