Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids

Thomas, Pete; Dominy, Peter; Vigh, László Gergely; Mansourian, Azad Reza; Quinn, Peter J.; Williams, W.P.

doi:10.1016/0005-2728(86)90104-0

Cited by 97 publications

(44 citation statements)

References 31 publications

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“…3A), assuming that TEMPO partitions badly into the H II phase of MGDG because of the tightly packed headgroup region in this structure (16). The temperature of this transition is known to decrease with increasing double bond content (52,53), but protein-lipid interactions may have an opposite effect by stabilizing MGDG in the bilayer (54,55). The characteristic temperature of this transition is highest (55°C) in the rearrangement phase in agreement with the protein-stabilizing structural role of MGDG (13,(54)(55)(56) and the largest protein-lipid interface.…”

Section: Discussionmentioning

confidence: 99%

Protein assembly and heat stability in developing thylakoid membranes during greening

Kóta

Horváth

Droppa

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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The development of the thylakoid membrane was studied during illumination of dark-grown barley seedlings by using biochemical methods, and Fourier transform infrared and spin label electron paramagnetic resonance spectroscopic techniques. Correlated, gross changes in the secondary structure of membrane proteins, conformation, composition, and dynamics of lipid acyl chains, SDS͞PAGE pattern, and thermally induced structural alterations show that greening is accompanied with the reorganization of membrane protein assemblies and the protein-lipid interface. Changes in overall membrane fluidity and noncovalent proteinlipid interactions are not monotonic, despite the monotonic accumulation of chlorophyll, LHCII [light-harvesting chlorophyll a͞b-binding (polypeptides) associated with photosystem II] apoproteins, and 18:3 fatty acids that follow a similar time course with highest rates between 12-24 h of greening. The 18:3 fatty acid content increases 2.8-fold during greening. This appears to both compensate for lipid immobilization by membrane proteins and facilitate packing of larger protein assemblies. The increase in the amount of protein-solvating immobile lipids, which reaches a maximum at 12 h, is caused by 40% decrease in the membranous mean diameter of protein assemblies at constant protein͞lipid mass ratio. Alterations in the SDS͞PAGE pattern are most significant between 6 -24 h. The size of membrane protein assemblies increases Ϸ4.5-fold over the 12-48-h period, likely caused by the 2-fold gain in LHCII apoproteins. The thermal stability of thylakoid membrane proteins increases monotonically, as detected by an increasing temperature of partial protein unfolding during greening. Our data suggest that a structural coupling between major protein and lipid components develops during greening. This protein-lipid interaction is required for the development and protection of thylakoid membrane protein assemblies.barley (Hordeum vulgare) ͉ FTIR ͉ photosynthesis ͉ protein-lipid interaction ͉ spin label EPR

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Section: Discussionmentioning

confidence: 99%

Protein assembly and heat stability in developing thylakoid membranes during greening

Kóta

Horváth

Droppa

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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“…In a direct test of this hypothesis, Thomas et al. (30) employed catalytic hydrogenation of pea thylakoids to alter the degree of lipid unsaturation. Comparisons of the effect of temperature on Chl fluorescence and freeze-fracture studies of hydrogenated and control membranes were consistent with the concept that lipid unsaturation plays a direct role in thermal stability of the membranes.…”

Section: Enhanced Thermal Tolerancementioning

confidence: 99%

Enhanced Thermal Tolerance of Photosynthesis and Altered Chloroplast Ultrastructure in a Mutant of Arabidopsis Deficient in Lipid Desaturation

Hugly

Kunst²,

Browse³

et al. 1989

Plant Physiol.

148

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A mutant of Arabidopsis thaliana, deficient in activity of the chloroplast n-6 desaturase, accumulated high levels of C16:1 and C18:1 lipids and had correspondingly reduced levels of polyunsaturated lipids. The altered lipid composition of the mutant had pronounced effects on chloroplast ultrastructure, thylakoid membrane protein and chlorophyll content, electron transport rates, and the thermal stability of the photosynthetic membranes. The change in chloroplast ultrastructure was due to a 48% decrease in the amount of appressed membranes that was not compensated for by an increased amount of nonappressed membrane. This resulted in a net loss of 36% of the thylakoid membrane per chloroplast and a corresponding reduction in chlorophyll and protein content. Electrophoretic analysis of the chlorophyll-protein complexes further revealed a small decrease in the amount of light-harvesting complex. Relative levels of whole chain and protosystem 11 electron transport rates were also reduced in the mutant. In addition, the mutation resulted in enhanced thermal stability of photosynthetic electron transport. These observations suggest a central role of polyunsaturated lipids in determining chloroplast structure and maintaining normal photosynthetic function and demonstrate that lipid unsaturation directly affects the thermal stability of photosynthetic membranes.The photosynthetic membranes of higher plants contain an unusually high proportion of polyunsaturated fatty acids.Depending on the plant species, trienoic acids (C16:3 and C18:3) and dienoic acids (C162 and C182) may account for 85% of the total fatty acids found within the chloroplast (1 1

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“…However, it remains unclear whether these factors are involved in the enhancement of thermal stability of the PSII complex during acclimation to high temperatures. Some researchers correlated the thermal stability of the PSII complex with levels of saturated membrane lipids in terms of acclimation to high temperature (Pearcy, 1978;Raison et al, 1982;Thomas et al, 1986). However, studies of mutant cyanobacteria defective in the desaturation of fatty acids provided direct evidence that contradicted previous suggestions that saturated lipids might be important in the thermal stability of the oxygen-evolving machinery (Gombos et al, 1991(Gombos et al, , 1994Mamedov et al, 1993;Wada et al, 1994;Moon et al, 1995).…”

mentioning

confidence: 99%

PsbU, a Protein Associated with Photosystem II, Is Required for the Acquisition of Cellular Thermotolerance inSynechococcus species PCC 70021

1999

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as assessed in terms of the levels of homologs of the heat-shock proteins Hsp60, Hsp70, and Hsp17, was unaffected by the mutation in psbU, suggesting that heat-shock proteins were not involved in the changes in the acclimative responses. Our observations indicate that PsbU is involved in the mechanism that underlies the enhancement of the thermal stability of the oxygen-evolving machinery and that the stabilization of the oxygen-evolving machinery is crucial for the acquisition of cellular thermotolerance.

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Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids

Cited by 97 publications

References 31 publications

Protein assembly and heat stability in developing thylakoid membranes during greening

Protein assembly and heat stability in developing thylakoid membranes during greening

Enhanced Thermal Tolerance of Photosynthesis and Altered Chloroplast Ultrastructure in a Mutant of Arabidopsis Deficient in Lipid Desaturation

PsbU, a Protein Associated with Photosystem II, Is Required for the Acquisition of Cellular Thermotolerance inSynechococcus species PCC 70021

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