Characterization of chloroplast photosystems 1 and 2 separated by a non-detergent method

Sane, P. V.; Goodchild, D. J.; Park, R.B.

doi:10.1016/0005-2728(70)90168-4

Cited by 304 publications

(85 citation statements)

References 19 publications

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“…If the primary thylakoids in the unfused stacks are comparable to the stroma lamellae of normal chloroplasts, the work of Sane et al (18) suggests that the leaves greened in far red light might be enriched in photosystem 1 activity. Previous low temperature absorption and derivative spectra of chloroplasts and of photosystems 1 and 2 subchloroplast particles obtained by digitonin fractionation showed that the long wavelength forms of chlorophyll, especially the 684, 690, and 698 nm-absorbing forms are associated with photosystem 1 particles (6).…”

Section: Discussionmentioning

confidence: 99%

Greening of Etiolated Bean Leaves in Far Red Light

1971

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Eight-day-old dark-grown bean leaves were greened by prolonged irradiation with far red light. Growth, chlorophyll content, oxygen-evolving capacity, photophosphorylation capacity, chloroplast structure (by electron microscopy), and in vivo forms of chlorophyll (by low temperature absorption and derivative spectroscopy on intact leaves) were followed during the greening process. Chlorophyll a accumulated slowly but continuously during the 7 days of the experiment (each day consisted of 12 hours of far red light and 12 hours of darkness). Chlorophyll b was not detected until the 5th day. The capacity for oxygen evolution and photophosphorylation began at about the 2nd day. Electron microscopy showed little formation of grana during the 7 days but rather unfused stacks of primary thylakoids. The thylakoids would fuse to give grana if the leaves were placed subsequently in white light.The low temperature spectroscopy of intact leaves showed that the chlorophyll a was differentiated into three forms with absorption maxima near 670, 677, and 683 nanometers at -196 C during the first few hours and that these forms accumulated throughout the greening process. Small amounts of two longer wavelength forms with maxima near 690 and 698 nanometers appeared at about the same time as photosynthetic activity.The development of etiolated tissue of higher plants in the light involves phototransformations of both phytochrome and protochlorophyll. Phytochrome controls a number of developmental processes from the synthesis of specific proteins (14) to the gross morphological characteristics such as leaf expansion (15). The development of photosynthetically active plastids, however, requires the phototransformation of protochlorophyll and the accumulation of chlorophyll. Even though both pigment systems play decisive roles in directing the development of the plant, there appears to be little interaction between the two systems with the exception that the rate of protochlorophyll synthesis after the initial transformation is influenced by phytochrome (16). Long before the discovery of phytochrome as the photomorphogenic pigment (5) of California, San Diego, La Jolla, California 92037 sources of different spectral quality and red and blue sources of low intensity, that protochlorophyll and chlorophyll did not participate in the photomorphogenic growth responses.Phytochrome in dark-grown seedlings is entirely in the Pr' form (3). It was shown, however, that a low level of Pfr is established as a photostationary state by far red light (because of the long wavelength absorption tail of Pr), and it was suggested that the photomorphogenic responses obtained with prolonged far red irradiation were due to the maintenance of the low level of Pfr over a long period of time (in darkness Pfr reverts to Pr) (3). Mohr and his co-workers (13) have shown in a number of cases that prolonged irradiation with far red light activates the phytochrome system. Hicker (9) illuminated etiolated mustard seedlings with continuous far red light (740 nm ...

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Section: Discussionmentioning

confidence: 99%

Greening of Etiolated Bean Leaves in Far Red Light

1971

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“…The distribution of the cytb 6 f complexes between the grana and stromal lamellae is much less clear. Biochemical evidence obtained on thylakoids fractionated either mechanically or with the detergent digitonin suggested that cytb 6 f was distributed fairly evenly between the grana and stromal lamellae (Boardman and Anderson, 1967;Sane et al, 1970;Cox and Andersson, 1981;Anderson, 1982;Dunahay et al, 1984). This even distribution was supported by immunogold labeling of the cytb 6 f complex in intact thylakoids and by freezefracture electron microscopy studies comparing the wild type and a cytb 6 f-less mutant of the green alga Chlamydomonas reinhardtii (Allred and Staehelin, 1985;Olive et al, 1986;Vallon et al, 1991;Hinshaw and Miller, 1993).…”

Section: Introductionmentioning

confidence: 88%

Nanodomains of Cytochromeb 6 fand Photosystem II Complexes in Spinach Grana Thylakoid Membranes

et al. 2014

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The cytochrome b 6 f (cytb 6 f) complex plays a central role in photosynthesis, coupling electron transport between photosystem II (PSII) and photosystem I to the generation of a transmembrane proton gradient used for the biosynthesis of ATP. Photosynthesis relies on rapid shuttling of electrons by plastoquinone (PQ) molecules between PSII and cytb 6 f complexes in the lipid phase of the thylakoid membrane. Thus, the relative membrane location of these complexes is crucial, yet remains unknown. Here, we exploit the selective binding of the electron transfer protein plastocyanin (Pc) to the lumenal membrane surface of the cytb 6 f complex using a Pc-functionalized atomic force microscope (AFM) probe to identify the position of cytb 6 f complexes in grana thylakoid membranes from spinach (Spinacia oleracea). This affinity-mapping AFM method directly correlates membrane surface topography with Pc-cytb 6 f interactions, allowing us to construct a map of the grana thylakoid membrane that reveals nanodomains of colocalized PSII and cytb6f complexes. We suggest that the close proximity between PSII and cytb 6 f complexes integrates solar energy conversion and electron transfer by fostering short-range diffusion of PQ in the protein-crowded thylakoid membrane, thereby optimizing photosynthetic efficiency.

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“…Photosystem 1 enriched membranes were prepared from isolated thylakoids by Yeda press treatment essentially according to the method of Sane et al (1970). Thylakoid membranes were resuspended in stacking medium (330 mM sorbitol, 5 mM MgCl,, 15 mM NaC1, 50 mM HEPES, pH 7.0) and incubated in the dark at 4 OC for 90 min.…”

Section: Biochemistrymentioning

confidence: 99%

Phase-controlled nonlinear interferometry

1989

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Lipid-protein interactions in thylakoid membranes, and in the subthylakoid membrane fractions containing either photosystem 1 or photosystem 2, have been studied by using spin-labeled analogues of the thylakoid membrane lipid components, monogalactosyldiacylglycerol, phosphatidylglycerol, and phosphatidylcholine. The electron spin resonance spectra of the spin-labeled lipids all consist of two components, one corresponding to the fluid lipid environment in the membranes and the other to the motionally restricted membrane lipids interacting directly with the integral membrane proteins. Spectral subtraction has been used to quantitate the fraction of the membrane lipids in contact with the membrane proteins and to determine the selectivity between the different lipid classes for the lipid-protein interaction. The fractions of motionally restricted lipid in the thylakoid membrane are 0.36, 0.39, and 0.53, for the spin-labeled monogalactosyldiacylglycerol, phosphatidylcholine, and phosphatidylglycerol, respectively. Spin-labeled monogalactosyldiacylglycerol exhibits very little preferential interaction over phosphatidylcholine, which suggests that part of the role of monogalactosyldiacylglycerol in thylakoid membranes is structural, as is the case for phosphatidylcholine in mammalian membranes. Spin-labeled phosphatidylglycerol shows a preferential interaction over the corresponding monogalactosyldiacylglycerol and phosphatidylcholine analogues, in contrast to the common behavior of this lipid in mammalian systems. This pattern of lipid selectivity is preserved in both the photosystem 1 and photosystem 2 enriched subthylakoid membrane fractions.T e photosynthetic apparatus of green plants comprises a series of integral protein complexes embedded in the thylakoid membrane. The conversion of light energy into a chemically useful form takes place at two reaction centers, photosystem 1 (PSI)' and photosystem 2 (PS2), which consist of complexes of different integral proteins. In the thylakoids from the mesophyll cells of higher plants, the two reaction centers and associated protein complexes are separately located in the appressed (PS2) and nonappressed (PSI) membrane regions. The appressed membranes are arranged in stacks and are interconnected by the nonappressed membranes, which contain regions of high membrane curvature. Within the thylakoid,

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Characterization of chloroplast photosystems 1 and 2 separated by a non-detergent method

Cited by 304 publications

References 19 publications

Greening of Etiolated Bean Leaves in Far Red Light

Greening of Etiolated Bean Leaves in Far Red Light

Nanodomains of Cytochromeb 6 fand Photosystem II Complexes in Spinach Grana Thylakoid Membranes

Phase-controlled nonlinear interferometry

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