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At least 19 recordsLinked to original sources

Role of Galactolipids in Spinach Chloroplast Lamellar Membranes: II. Effects of Galactolipid Depletion on Phosphorylation and Electron Flow.

A galactolipid lipase from primary bean (Phaseolus vulgaris) leaves has been used to partially deplete spinach chloroplast inner membranes of their galactolipids. Chloroplasts treated with the lipase in the absence of bovine serum albumin lost 91% of their monogalactosyl diglyceride, 83% of their digalactosyl diglyceride, all of their phosphatidyl choline, but none of their sulfolipid. Electron microscopy of this sections revealed that the treated chloroplasts were greatly enlarged and lacked membrane stacking. Linolenic acid had similar effects on the structure of the chloroplasts. Chlorophyll, carotenoids, and coupling factor 1 remained bound to the treated membranes.To minimize the inhibition of phosphorylation and electron flow by fatty acids released by the lipase, bovine serum albumin (15-24 mg/ml) was added to the lipase incubation mixtures. Bovine serum albumin inhibited the extent, but not the initial rate, of fatty acid release by the lipase. Electron microscopy of chloroplasts treated with the lipase in the presence of bovine serum albumin showed that membrane stacking was partially maintained. Chloroplasts treated with lipase under these conditions retained about 30% of their monogalactosyl diglyceride, 50% of their digalactosyl diglyceride and phosphatidyl choline. The sulfolipid and phosphatidyl glycerol contents were unchanged. Electron flow through photosystems I and II with artificial electron donors and acceptors was not affected by lipase treatment in the presence of bovine serum albumin. In contrast, oxygen evolution and phosphorylation were partially inhibited. These reactions are also very sensitive to fatty acids and it is possible that the inhibition is the result of interaction of fatty acids with the membrane prior to their binding to bovine serum albumin.In view of the irreversible inactivation of electron flow and phosphorylation by fatty acids, it is difficult to assess the role of galactolipids in these processes when a specfic lipase is used to deplete the membrane.

Journal Article↗

Galactolipid formation in chloroplast envelopes. II. Isolation-induced changes in galactolipid composition.

Spinach envelopes were isolated at pH 8.5, which is inhibitory to interlipid galactosyl transfer, and at pH 7.2, which is close to values used in most recent work on chloroplast envelopes. Peptide patterns were identical, but galactolipid compositions differed markedly. These changes are such as could be explained by interlipid galactosyl transfer during isolation at pH 7.2, i.e. a strong decrease in monogalactolipid and a corresponding increase in tri- and tetragalactolipids and diacylglycerol. Digalactolipid was little affected. It was further observed that the interlipid galactosyl transfer was restricted to lipids rich in hexadecatrienoic acid. Arguments are presented that the lipid composition of envelopes in vivo is better represented by the results obtained at high pH. The results will be discussed in relation to previous data on galactolipid composition and biosynthesis in envelopes.

Chloroplasts↗

The role of galactolipids in spinach chloroplast lamellar membranes: I. Partial purification of a bean leaf galactolipid lipase and its action on subchloroplast particles.

A galactolipid lipase has been isolated and partially purified from the chloroplast fraction of the primary leaves of Phaseolus vulgaris var. Kentucky Wonder. The lipase hydrolyzed monogalactosyl diglyceride rapidly and phosphatidyl choline relatively slowly. Triolein and p-nitrophenyl stearate were not hydrolyzed.Spinach subchloroplast particles were excellent substrates for the lipase. Initial rates of fatty acid release from subchloroplast particles at 30 C by the lipase as high as 60 microequivalents per minute per milligram protein were observed. At completion of the reaction, about 2.7 microequivalents of fatty acid were liberated per milligram of chlorophyll in the subchloroplast particles, indicating that major amounts of lipid in the particles were rapidly attacked by the lipase.The treatment of subchloroplast particles with the lipase resulted in a rapid inhibition of light-dependent electron flow. This inhibition was largely prevented when the incubation was carried out in the presence of high concentrations of defatted bovine serum albumin. These results suggest that when precautions are taken to prevent the binding of fatty acids to the subchloroplast particles, large amounts of lipid may be removed without a marked effect on electron flow.

Journal Article↗

Galactolipid Synthesis in Vicia faba Leaves: II. Formation and Desaturation of Long Chain Fatty Acids in Phosphatidylcholine, Phosphatidylglycerol, and the Galactolipids.

The labeling kinetics of the fatty acids of phosphatidylcholine (PC), phosphatidylglycerol (PG), monogalactosyldiglyceride (MGDG), and digalactosyldiglyceride (DGDG) were examined after (14)CO(2) feeding and incubation of leaf discs of Vicia faba over 72 hours in continuous light. The results indicate a rapid accumulation and turnover of radioactivity into PC and PG fatty acids (oleic acid in PC and oleic and palmitic acids in PG). Radioactivity accumulates in MGDG and DGDG fatty acids much more slowly and continuously over 72 hours. Most of this activity is found in linoleic and linolenic acids; very little activity is found in the more saturated fatty acids. Little or no desaturation occurs in situ in conjunction with the galactolipids. The results suggest that PC and PG may act as "carriers" for MGDG and DGDG fatty acid synthesis. Analyses of the labeling patterns of the molecular species of MGDG after (14)CO(2) and (14)C-acetate feeding confirm that MGDG is formed by galactosylation of a preformed diglyceride containing predominantly unsaturated fatty acids.

Journal Article↗

Lead exposure affects levels of galactolipid metabolic enzymes in the developing rat brain.

Lead poisoning is known to cause myelin defects. Galactolipids are the major lipid components of myelin and myelin-competent oligodendrocytes. The present study examines the cellular activity of enzymes involved in the galactolipid pathway, tissue concentrations of galactolipids, and the cellular activity of 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNPase) in rat pups exposed to lead in utero and subsequently through maternal milk from exposed mothers and in drinking water following weaning. Pups from control and lead-treated groups (500 or 2000 ppm lead in the drinking water) were euthanized by decapitation on postnatal day 7, 14, 21, 35, or 56. Lead decreased levels of galactolipids and the oligodendrocyte marker CNPase in the brain to a similar degree. The ratios of galactocerebrosides/sulfatides and nonhydroxy fatty acid/hydroxy fatty acid forms of the galactolipids were not altered by lead treatment. In contrast, the activities of the galactolipid metabolic enzymes were reduced to a degree significantly greater than that of CNPase or galactolipids. These results are consistent with previously obtained data indicating that in vitro cultured oligodendroglial progenitor cells are a target for Pb toxicity. Chronic Pb exposure may impact on brain development by impairing timely myelin production due to perturbation of the early developmental commitment of oligodendroglial progenitors. It is further suggested that perturbation of the galactolipid pathway during the developmental maturation of oligodendrocytes may represent a contributing mechanism for Pb-induced neurotoxicity.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗

Galactosyltransferases involved in galactolipid biosynthesis are located in the outer membrane of pea chloroplast envelopes.

The galactosylation steps in the biosynthesis of galactolipids involve two different enzymes; a UDP-Gal:diacylglycerol galactosyltransferase and a galactolipid:galactolipid galactosyltransferase. Previous localization studies have shown that in spinach these enzymes are located in the chloroplast envelope. Our results with peas (Pisum sativum var Laxton's Progress No. 9) confirm these results and extend the localization by providing evidence that the galactosyltransferases are in the outer membrane of the envelope. The specific activity of UDP-Gal:diacylglycerol galactosyltransferase in outer membrane preparations was 6 to 10 times greater than that exhibited by inner membrane preparations. In addition, using quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it was possible to show that the UDP-Gal:diacylglycerol galactosyltransferase activity associated with inner membrane preparations could be accounted for by outer membrane contamination. It is concluded from these results that this enzyme is located predominantly, if not exclusively, in the outer membrane of the envelope. An analysis of the galactolipid products synthesized by the highly purified outer membrane showed that the galactolipid:galactolipid galactosyltransferase is also present, suggesting that this enzyme is also an outer membrane enzyme. The implication of these results is that the final assembly of galactolipids is carried out on the outer membrane of the chloroplast envelope.

Journal Article↗

Galactolipids rule in seed plants.

Chloroplast membranes contain high levels of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG). The isolation of the genes involved in the biosynthesis of MGDG and DGDG, and the identification of galactolipid-deficient Arabidopsis mutants has greatly facilitated the analysis of galactolipid biosynthesis and function. Galactolipids are found in X-ray structures of photosynthetic complexes, suggesting a direct role in photosynthesis. Furthermore, galactolipids can substitute for phospholipids, as suggested by increases in the galactolipid:phospholipid ratio after phosphate deprivation. The ratio of MGDG to DGDG is also crucial for the physical phase of thylakoid membranes and might be regulated.

Arabidopsis↗

Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis.

Two genes (DGD1 and DGD2) are involved in the synthesis of the chloroplast lipid digalactosyldiacylglycerol (DGDG). The role of DGD2 for galactolipid synthesis was studied by isolating Arabidopsis T-DNA insertional mutant alleles (dgd2-1 and dgd2-2) and generating the double mutant line dgd1 dgd2. Whereas the growth and lipid composition of dgd2 were not affected, only trace amounts of DGDG were found in dgd1 dgd2. The growth and photosynthesis of dgd1 dgd2 were affected more severely compared with those of dgd1, indicating that the residual amount of DGDG in dgd1 is crucial for normal plant development. DGDG synthesis was increased after phosphate deprivation in the wild type, dgd1, and dgd2 but not in dgd1 dgd2. Therefore, DGD1 and DGD2 are involved in DGDG synthesis during phosphate deprivation. DGD2 was localized to the outer side of chloroplast envelope membranes. Like DGD2, heterologously expressed DGD1 uses UDP-galactose for galactosylation. Galactolipid synthesis activity for monogalactosyldiacylglycerol (MGDG), DGDG, and the unusual oligogalactolipids tri- and tetragalactosyldiacylglycerol was detected in isolated chloroplasts of all mutant lines, including dgd1 dgd2. Because dgd1 and dgd2 carry null mutations, an additional, processive galactolipid synthesis activity independent from DGD1 and DGD2 exists in Arabidopsis. This third activity, which is related to the Arabidopsis galactolipid:galactolipid galactosyltransferase, is localized to chloroplast envelope membranes and is capable of synthesizing DGDG from MGDG in the absence of UDP-galactose in vitro, but it does not contribute to net galactolipid synthesis in planta.

Alleles↗

Myelin-associated galactolipids in primary cultures from dissociated fetal rat brain: biosynthesis, accumulation, and cell surface expression.

Galactolipid metabolism was investigated as a function of development in primary cultures initiated from 19-21-day-old dissociated fetal rat brain. Significant amounts of galactocerebrosides, sulfatides, and monogalactosylglycerides were synthesized and accumulated by 8 days in culture. Thereafter the synthetic rates and levels of these galactolipids increased rapidly, reaching maximal values approximately 22-29 days in culture. Galactolipids containing nonhydroxy or 2-hydroxy fatty acid were both synthesized at approximately equal rates. The initial rates of synthesis, investigated at 15, 29, and 50 days in culture, were three- to fivefold higher for galactocerebrosides than for sulfatides and two- to threefold higher than for monogalactosylglycerides. The total number of cells staining with antisera against galactocerebroside of sulfatide also increased very rapidly between 8 and 22 days in culture, reaching levels of 4-5 million cells per seeded fetal brain. The amount of galactocerebroside or sulfatide per cell stained with the corresponding antiserum increased severalfold from 10 to 27 days in culture and remained high until at least 36 days in culture (the latest time point examined). Thus, the temporal expression of galactolipid accumulation in the cell cultures was comparable to that occurring in rat brain, but some important quantitative reductions in the levels of accumulation per cell in culture were noted. In addition, in contrast to normal brain in which galactolipid synthetic rates are reduced after the period of most active myelination, in culture both synthesis and turnover of these galactolipids remained high, suggestive of a partial arrest in myelin maturation.

Animals↗

Dynamics of Galactolipids and Plastids in Nonphotosynthetic Cells of Glycine max Suspension Cultures : A Morphological and Biochemical Study.

The age-dependent interrelationship of galactolipids and plastids in heterotrophic cell suspension cultures of Glycine max (soybean) was studied with regard to aging of nonphotosynthetic cells. Cells were propagated in the dark and under illumination with white light, and were harvested at days 7 (end of logarithmic phase), 14, and 21 (extended stationary phase). Electron microscopy revealed in dark-grown cells a proliferating decay of the amyloplast-type plastids, which could be correlated to a decrease of galactolipids. This trend was dramatically reversed in irradiated cultures, where the plastids of day 21 cells appeared rejuvenated. A concomitant increase of galactolipid content in the cells was observed, yet chlorophyll synthesis and photosynthetic activity were not induced. The dynamics of galactolipid contents did not correlate with total lipid contents in dark-grown as well as in irradiated cultures. [(3)H]Galactose served as a radioactive probe for the subcellular localization of galactolipids by electron microscopic autoradiography. Apart from plastids, galactolipids may also be constituents of the plasma membrane. The results render the heterotrophic cell suspension culture a suitable model to study the impact of senescence on plastids of nonphotosynthetic cells.

Journal Article↗

Biosynthesis of galactolipids by enzyme preparations from spinach leaves.

The pH optimum for galactolipid synthesis from UDP-galactose by spinach chloroplasts is 7.2 in Tris-HCl or phosphate buffer. The products include sterol glycosides, trigalactosyl diglyceride (tentatively identified), digalactosyl diglyceride, and monogalactosyl diglyceride in increasing order of quantity. The proportion of monogalactosyl diglyceride decreases and that of digalactosyl diglyceride increases as the pH is lowered. The galactolipid synthesis is quite resistant to elevated temperature; maximal incorporation of galactose from UDP-galactose was observed at 45 degrees C. The proportion of monogalactosyl diglyceride was greater at the higher temperatures. As much as 40% of the galactolipid-synthesizing capability of a spinach leaf homogenate is not sedimented by centrifugation for 60 min at 100,000 g. An acetone powder of spinach chloroplasts contains enzymes which catalyze galactolipid synthesis. This preparation is dependent on added diglycerides in order to make galactolipid, whereas the chloroplast preparation is not dependent on added diglycerides. Molecular species of diglycerides were compared as requirements for galactolipid synthesis. The requirement was satisfied best by the diglycerides of highest unsaturation. Methylation of the free hydroxyl of the diglyceride eliminated the effectiveness.

Chloroplasts↗

Isolation and structure of a new galactolipid from oat seeds.

Seeds of oat (Avena sativa L.) were recently shown to contain significant quantities of a new hydroxy acid, (15 R)-hydroxy-(9Z),(12Z)-octadecadienoic acid (trivial name, avenoleic acid). In the present work, avenoleate was found to be mainly (63%) localized in the glycolipid fraction of oat seed lipids. Fractionation of the glycolipids by thin-layer chromatography and reversed-phase high-performance liquid chromatography revealed the presence of a main molecular species which accounted for 20% of the total avenoleate content of oat seeds. Structural studies by chemical methods and mass spectrometry demonstrated that the avenoleate-containing glycolipid was a galactolipid assembled of one molecule of avenoleic acid, two molecules of linoleic acid, two molecules of D-galactose, and one molecule of glycerol. Degradation of the new galactolipid by chemical and enzymatic methods demonstrated the localization of acyl chains, i.e., linoleate at sn-1 and linoleoylavenoleate at sn-2. Nuclear magnetic resonance spectroscopy gave independent support for this structure and also demonstrated that the two galactoses formed an alpha-D-galactopyranosyl-1-6-beta-D-galactopyranosyl moiety which was bound to the sn-3 position. Based on these experiments, the new galactolipid could be formulated as 1-[(9'Z),(12'Z)-octadecadienoyl]-2-[(15''R)-[(9'''Z),(12'''Z)-o ctadecadienoyloxy]-(9''Z),(12''Z)-octadecadienoyl]-3-(alpha-D-g alactopyranosyl-1-6-beta-D-galactopyranosyl)-glycerol. Quantitatively, the amount of the avenoleate-containing galactolipid was of the same order of magnitude as those of individual molecular species of digalactosyldiacylglycerol containing nonoxygenated acyl chains. The content of the new galactolipid in oat seeds was 0.5-0.6 mg per g of seed.

Avena↗

Green light for galactolipid trafficking.

Galactolipids not only play a crucial role in photosynthesis but are also important for the adaptation of membrane-lipid composition in plants to phosphate-limiting conditions. The enzymes of galactolipid assembly have been localised to the envelope membranes of chloroplasts. Lipid trafficking is essential for galactolipid synthesis and redistribution because lipid precursors originate from two compartments, the endoplasmic reticulum (ER) and the plastid, and because galactolipids have to be transported to extraplastidial membranes during phosphate deprivation. Analysis of Arabidopsis mutants that are impaired in galactolipid synthesis (i.e. dgd1 and dgd2) or in ER-to-plastid lipid transport (i.e. tgd1) has resulted in the identification of a processive galactosyltransferase whose function is still enigmatic.

Arabidopsis↗

Lead alters the developmental profile of the galactolipid metabolic enzymes in cultured oligodendrocyte lineage cells.

Lead is a neurotoxicant that can cause myelin deficits. Galactolipids are expressed during differentiation of oligodendrocyte lineage cells and accumulate in myelin. To examine the impact of lead on oligodendroglial differentiation, galactolipid metabolism in cultured oligodendrocyte lineage cells exposed to the metal was studied. Oligodendrocyte progenitor cells obtained from newborn rat pups were exposed to 1 microM lead acetate for 24 h prior to maintenance of the cells in medium containing the metal salt for 0, 2, or 6 days of differentiation. Lead caused approximately 50% reduction in levels of the galactolipid biosynthetic transferases, UDP-galactose:ceramide galactosyltransferase and 3'-phosphoadenosine-5'-phosphosulfate:galactocerebroside sulfotransferase, as compared to sodium-treated controls, in cultures of oligodendrocyte lineage cells following 2 days of differentiation. The activities of the galactolipid catabolic hydrolases, galactocerebroside-beta-galactosidase and arylsulfatase A, were reduced by 20%. Following 6 days of differentiation, lead-exposed cells exhibited levels of all the enzymes, except for arylsulfatase A, similar to those of the control cells. These results are consistent with the lead-induced delay of oligodendrocyte differentiation, as evidenced by the emergence of stage-specific immunochemical markers and the observed change in the developmental activity profile of 2',3'-cyclic nucleotide 3'-phosphohydrolase. The activity of arylsulfatase A in lead-treated 6-day oligodendrocytes was significantly less than that found in control cultures. This effect is consistent with the lead-induced reduction of arylsulfatase A in human fibroblasts caused by mis-sorting the newly-synthesized enzyme. The perturbation of galactolipid metabolism by lead during developmental maturation of oligodendrocytes may represent a contributing mechanism for lead-induced neurotoxicity.

Animals↗

A re-examination in vivo of the phosphatidylcholine-galactolipid metabolic relationship during plant lipid biosynthesis.

It remains unclear how and in what form the lipids synthesized in plant endoplasmic reticulum are exported to chloroplasts and used as precursors for the biosynthesis of plastid galactolipids, which are the most abundant lipids on Earth. Neither the mechanism of transfer nor the nature of the lipids imported into plastids has been elucidated. To characterize events occurring in vivo, the labelling of lipids from 15-day-old leek seedlings (Allium porrum, var. furor) was studied using pulse-chase experiments. During the chase, a substantial decline in the radioactivity incorporated into phosphatidylcholine (and not in other phospholipids) was accompanied by an increase in the label found in galactolipids. The positional distribution of labelled fatty acids in phosphatidylcholine and galactolipids was further studied as a function of the chase time; whereas phosphatidylcholine was preferentially labelled at the sn-2 position, the increase in radioactivity in galactolipids mainly concerned the sn-1 position. These results strongly suggest that the diacylglycerol moiety of phosphatidylcholine might not be integrated as a whole in the galactolipid.

Carbon Radioisotopes↗

Membrane composition can influence the rate of Al3+-mediated lipid oxidation: effect of galactolipids.

In the first part of the present study we investigated the effects of pre-natal and early postnatal exposure of mice to high levels of dietary Al3+ on myelin lipid composition and lipid oxidation. We found: (1) a significantly higher (104%; P<0.01) content of brain myelin galactolipids in the high-Al3+ group than in controls, and, (2) a significant correlation (r2=0.70; P<0.01) between the concentration of myelin galactolipids and TBARS (2-thiobarbituric acid-reactive substances) content, a parameter of lipid oxidation. Based on these results, we evaluated in an in vitro model (liposomes) whether galactolipids could affect the capacity of Al3+ to stimulate Fe2+-initiated lipid oxidation, and whether this effect could be due to the promotion of changes in membrane physical properties (membrane phase separation and rigidification). The presence of galactolipids (10-40 mol%) in the liposomes caused a concentration-dependent increase in the stimulatory effect of Al3+ on Fe2+-induced TBARS production, and on the ability of Al3+ to induce phase separation and membrane rigidification. The capacity of Al3+ (10-100 microM) to induce lateral phase separation in liposomes composed of phosphatidylcholine/phosphatidylserine/galactolipid (36:24:40, molar ratio) was correlated significantly (r2=0.99; P<0. 001) with the stimulatory action of Al3+ on Fe2+-induced TBARS production. We propose that the high content of galactolipids found in myelin from Al3+-intoxicated mice could favour Al3+-induced changes in membrane physical properties, with the subsequent acceleration of lipid oxidation rates.

Aluminum↗

DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis.

The galactolipids, mono- and digalactosyldiacylglycerol (DGDG), are the most common nonphosphorous lipids in the biosphere and account for 80% of the membrane lipids found in green plant tissues. These lipids are major constituents of photosynthetic membranes (thylakoids), and a large body of evidence suggests that galactolipids are associated primarily with plastid membranes in seed plants. A null-mutant of Arabidopsis (dgd1), which lacks the DGDG synthase (DGD1) resulting in a 90% reduction in the amount of DGDG under normal growth conditions, accumulated DGDG after phosphate deprivation up to 60% of the amount present in the wild type. This observation suggests the existence of a DGD1-independent pathway of galactolipid biosynthesis. The fatty acid composition of the newly formed DGDG was distinct, showing an enrichment of 16-carbon fatty acids in the C-1 position of the glycerol backbone of DGDG. Roots with their rudimentary plastids accumulated large amounts of DGDG after phosphate deprivation, suggesting that this galactolipid may be located in extraplastidic membranes. Corroborating evidence for this hypothesis was obtained directly by fractionation of subcellular membranes from leaf tissue and indirectly by lipid analysis of the phosphate-deprived fad3 mutant primarily deficient in extraplastidic fatty acid desaturation. The discovery of extraplastidic DGDG biosynthesis induced by phosphate deprivation has revealed a biochemical mechanism for plants to conserve phosphate. Apparently, plants replace phospholipids with nonphosphorous galactolipids if environmental conditions such as phosphate deprivation require this for survival.

Arabidopsis↗

The effects of galactolipid depletion on the structure of a photosynthetic membrane.

The galactolipids monogalactosyldiglyceride and digalactosyldiglyceride together comprise more than 77% of the photosynthetic membrane lipids of higher plant chloroplasts. We have isolated a lipase from the chloroplasts of runner beans (Phaseolus vulgaris) which is highly specific for these galactolipids. This galactolipase promotes the hydrolysis of monogalactosyldiglyceride and digalactosyldiglyceride, in the process liberating two free fatty acids into the membrane bilayer, leaving the residual galactosyl glyceride group to diffuse into the aqueous bulk phase. Isolated spinach photosynthetic membranes were treated with this enzyme preparation and changes in membrane composition were studied with thin layer chromatography (for lipids), gel electrophoresis (proteins), and freeze-etching (membrane structure). After 30 min of lipolysis, nearly 100% of the galactolipids had been converted into membrane-associated fatty acids and water-soluble galactosyl glycerides. SDS PAGE showed that two proteins, one of which is possibly associated with the reaction center of photosystem II, were removed by the treatment. Despite the minor nature of changes in membrane protein composition, freeze-fracture and freeze-etch studies showed that striking changes in membrane structure had taken place. The large freeze-fracture particle on the E fracture face had disappeared in stacked regions of the membrane system. In addition, a tetrameric particle visible at the inner surface of the membrane had apparently dissociated into individual monomeric particles. The fact that these two structures are so dramatically affected by the loss of galactolipids strongly suggests that these lipids play a crucial role in maintaining their structure. Both structures are believed to be different views of the same transmembrane unit: a membrane-spanning complex associated with photosystem II. Our results are consistent with two possible interpretations: the intramembrane particles may be lipidic in nature, and hence lipolysis causes their disappearance; or galactolipids are necessary for the organization of a complex photosystem II-associated structure which is composed of a number of different molecular species.

Carboxylic Ester Hydrolases↗