Subunits in the membranes of chloroplasts of Phaseolus vulgaris, Pisum sativum, and Aspidistra sp.

TlIhe plant sulfolipid, 6-sulfo-a-D-quinovopyranosyl-( 1 --1') -2'-,3'-di-O-acyl-D-glycerol. has been found in high concentrations in all and only in photosynthetic 02-producing organisms yet investigated (5, 6). Shibuya and Hase (21) recently demonstrated the concerted changes in chloroplast development and sulfolipid content in a green alga, Chlorcla protothecoides. It is increasingly apparent that these surfactant lipids play an important role in chloroplast lipoprotein structure. For an intrinsic study of biochemistry of the sulfolipids, the localization of the compounds in the organelle is of obvious interest. The intracellular distribution of the sulfolipid has been studied (29, 30) but the difficulty of quantitatively isolating chloroplasts from photosynthetic tissues precluded assignment of their distribution within the cell on the basis of radioactivity measurements.In the present study, a radiochemical investigation on the distribution of various components was first conducted with the chloroplasts isolated from C14-labeled Lemnia perpiusilla. Since the lamellar fraction was found to represent practically whole chloroplasts, as far as the glycolipid contents were concerned, it seemed desirable to develop a procedure for the quantitative isolation of such chloroplast fragments from whole plant tissues. A radiochromatographic investigation of an S35-labeled preparation thus obtained has demonstrated the specific localization of the sulfolipids in the lamellar fragments, a particulate fraction from chloroplasts first described by Park and Pon (19,20) as containing pigments and part of the electron transport systems for photosynthesis. This paper reports the details of these experiments as well as of the chemical characterization of a spinach lamellar preparation, and discusses significance of the present findings.

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“…These facts are in accord with the proposed hydrophobic association model of the lamellar lipoprotein (7,27) …”

Section: Methodssupporting

confidence: 90%

Sulfolipid localization in lamellar lipoprotein.

Shibuya¹,

Maruo²,

Benson³

1965

Plant Physiol.

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“…In Phaseolus vulgaris these lamellae are porous and the prolamellar body arises through a contraction of these porous lamellae and the formation of interconnecting tubules linking each lamella to the one above it and the one below it. This paper reports the results of two experiments on changes in the prolamellar body of Phaeeolus vulgaris induced by light of less than 100 ft-c (Weier, Sjolund, and Butler, 1967). The results were completely unexpected and required supporting observations.…”

mentioning

confidence: 86%

“…Vesicle dispersal is independent of temperature while grana formation is temperature dependent (von Wettstein, 1967). Weier and Brown (1970) have followed the development of etioplasts in Phaseolus vulgaris from 3 to 8 days. They concurred with the report of Engelbrecht and Weier (1967) that sheets of membranes, rather than vesicles, arise from the inner component of the plastid envelope.…”

mentioning

confidence: 99%

“…Pieces l-mm" of the primary leaves were fixed in 5 % glutaraldehyde in 0.15 M phosphate buffer at pH 7.2 for 1 hr, washed thoroughly in buffer, and post-fixed in 1 % HOBO in 0.15 M phosphate buffer for 1~hr. Dehydration was by an ethanolpropylene oxide series followed by embedding in Maraglas (Weier et al, 1965). Sections were cut with a diamond knife on a Porter-Blum MTI microtome and stained with a 2 % aqueous uranyl acetate solution followed by lead citrate (Reynolds, 1963).…”

mentioning

confidence: 99%

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Changes Induced by Low Light Intensities on the Prolamellar Body of 8‐day, Dark‐grown Seedlings

Weier

Sjoland

Brown

1970

American J of Botany

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A B S T RAe T Etioplasts of 8-day-old, dark-grown seedlings of Phaseolus vulgaris contain large, crystalline prolamellar bodies. The basic structural unit within the prolamellar body is a six-pointed star (star module) with four tubules fusing at each of the nodes. With sufficient illumination some of the tubules are withdrawn and the crystalline prolamellar body transforms to a complex tangle of tubules, the reacted prolamellar body. In vivo spectrophotometry and electron microscopic observations were carried out on portions of the same leaves after varying periods of illumination with low light intensity. Protochlorophyllide transformation was normal. However, the structural changes are not closely tied to protochlorophyllide conversion. The pigment conversion is complete after 20 sec of illumination, but 80% of the prolamellar bodies are still in the crystalline form after 20 min of illumination. After 1 and 2 hr of illumination all prolamellar bodies are reacted. Mter 4 hr of continuous illumination 35%, and by 12 hr 60%, of the prolamellar bodies returned to the crystalline form. Spectrophotometric evidence and presence of grana show chlorophyll synthesis during this period. The' coexistence of grana and the crystalline prolamellar body indicates that when insufficient photosynthetic membrane constituents are provided by the photoreactions, under low light intensity, the membranes of the reacted prolamellar body will be forced to reform a crystalline prolamellar body.

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“…Fixations used were as follows: (1) phosphate-buffered (0.15 M, p H 7.1) 6% glutaraldehyde for 3.5 or 4 h followed, after washing, by phosphate-buffered ( After fixation, the tissue was washed in phosphate buffer, dehydrated in a graded ethanol series followed by several changes of propylene oxide, infiltrated, and embedded with epoxy resin. The epoxy resin was a 7:3 mixture of Maraglas-Cardolite (w/w) with 2% BDMA as initiator (Weier et al 1965). The tissue was infiltrated over several days through a graded propylene oxideresin series.…”

Section: Cf~etnical Fixation Of Tissuementioning

confidence: 99%

Protein bodies from the cotyledons of Cucurbita maxima

Lott¹,

Larsen²,

Darley³

1971

Can. J. Bot.

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1971. Protein bodies from the cotyledons of Cltcurbitn maxima. Can. J. Bot. 49: 1777-1782.The structure of protein bodies from cotyledon tissue of dormant squash seeds was studied using several different preparative techniques. Four major components, the proteinaceous matrix, the protein crystalloid, the soft globoid, and the globoid crystal were found and verified to be present in protein bodies from the large mesophyll cells. Some of these four components were found to be absent in protein bodies of epidermal cells or in protein bodies near the nucleus of mesophyll cells. The globoid crystal, which was hard and electron dense after osmium fixation, is probably the site of phytin storage. The globoid crystal was usually surrounded by the soft globoid, a material of undetermined composition which tended to smear during freeze-etching. Some protein bodies contained several of these globoid regions although most protein bodies seemed to have only one globoid region. One or several protein crystalloids were usually found in protein bodies. Both the protein crystalloids and the globoid regions were surrounded by a proteinaceous matrix substance.Glutaraldehyde-permanganate fixation of tissue clearly showed the presence of the proteinaceous ground substance and the protein crystalloid but the globoid structures were absent. In tissue chemically fixed with glutaraldehyde-osmium all four components were sometimes found but interpretation, on the basis of this fixation alone, was difficult because of the presence of fixation artifacts. Isolation of protein bodies from cotyledon tissue made faster and better quality osmium or glutaraldehyde-osmium fixations possible. In such protein body pellets all four components were seen. Freeze-etching of tissue verified the presence of the globoid crystal and the soft globoid in most protein bodies from cotyledon mesophyll cells. In dormant seed tissue the two proteinaceous components usually were not distinguishable by the freezeetching technique however. Thus only through the use of several different preparative techniques was it possible to locate and verify the presence of the various structural components in protein bodies from squash cotyledons.

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Subunits in the membranes of chloroplasts of Phaseolus vulgaris, Pisum sativum, and Aspidistra sp.

Cited by 54 publications

References 23 publications

Sulfolipid localization in lamellar lipoprotein.

Sulfolipid localization in lamellar lipoprotein.

Changes Induced by Low Light Intensities on the Prolamellar Body of 8‐day, Dark‐grown Seedlings

Protein bodies from the cotyledons of Cucurbita maxima

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