Preparation and Characterization of Membrane Fractions Enriched in Outer and Inner Envelope Membranes from Spinach Chloroplasts

Block, Maryse A.; Dorne, Albert-Jean; Joyard, Jacques; Douce, Roland

doi:10.1007/978-94-017-4973-2_5

Cited by 171 publications

(241 citation statements)

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“…The qualitative lipid composition as determined by onedimensional thin-layer chromatography (TLC) was also confirmed by two-dimensional TLC. The quantitative lipid composition of both chloroplasts and thylakoid fractions (Table I) were quite similar to previously published data on spinach (Spinacia oleracea; Block et al, 1983) and wheat thylakoids (Bahl et al, 1976). The percentage of PC, however, was somewhat lower in our thylakoid fractions and the PI content of the thylakoid fractions was too low to be reliably quantified (Ͻ0.5 mol %).…”

Section: Fraction Purity Of the Isolated Thylakoid Fractionssupporting

confidence: 70%

Chloroplast Biogenesis. Regulation of Lipid Transport to the Thylakoid in Chloroplasts Isolated from Expanding and Fully Expanded Leaves of Pea

2001

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To study the regulation of lipid transport from the chloroplast envelope to the thylakoid, intact chloroplasts, isolated from fully expanded or still-expanding pea (Pisum sativum) leaves, were incubated with radiolabeled lipid precursors and thylakoid membranes subsequently were isolated. Incubation with UDP[ 3 H]Gal labeled monogalactosyldiacylglycerol in both envelope membranes and digalactosyldiacylglycerol in the outer chloroplast envelope. Galactolipid synthesis increased with incubation temperature. Transport to the thylakoid was slow below 12°C, and exhibited a temperature dependency closely resembling that for the previously reported appearance and disappearance of vesicles in the stroma (D.J. Morré, G. Selldén, C. Sundqvist, A.S. Sandelius [1991] Plant Physiol 97: 1558-1564). In mature chloroplasts, monogalactosyldiacylglycerol transport to the thylakoid was up to three times higher than digalactosyldiacylglycerol transport, whereas the difference was markedly lower in developing chloroplasts. Incubation of chloroplasts with [ 14 C]acyl-coenzyme A labeled phosphatidylcholine (PC) and free fatty acids in the inner envelope membrane and phosphatidylglycerol at the chloroplast surface. PC and phosphatidylglycerol were preferentially transported to the thylakoid. Analysis of lipid composition revealed that the thylakoid contained approximately 20% of the chloroplast PC. Our results demonstrate that lipids synthesized at the chloroplast surface as well as in the inner envelope membrane are transported to the thylakoid and that lipid sorting is involved in the process. Furthermore, the results also indicate that more than one pathway exists for galactolipid transfer from the chloroplast envelope to the thylakoid.

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Section: Fraction Purity Of the Isolated Thylakoid Fractionssupporting

confidence: 70%

Chloroplast Biogenesis. Regulation of Lipid Transport to the Thylakoid in Chloroplasts Isolated from Expanding and Fully Expanded Leaves of Pea

2001

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“…Endomembrane analyses are derived from [102], [103], and [104]. Plastid and mitochondria membrane analyses were done respectively by [105] and [106]. synthesized in the chloroplast, formation of eukaryotic type galactolipids is dependent on the supply to the envelope of some PC derivatives formed in the ER: either diacylglycerol (DAG E) [6] or phosphatidate (PA E ) [37].…”

Section: Resultsmentioning

confidence: 99%

Glycerolipid transfer for the building of membranes in plant cells

Jouhet

Maréchal

Block

2007

Progress in Lipid Research

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131

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“…However, the protein composition of outer membranes is much simpler than that of inner membrane. The lipid to protein ratio of outer membrane is about 3 times higher than that of inner membrane and the inner envelope membrane, which contains various metabolite translocators, is the main permeability barrier for solutes, although there is growing evidence suggesting that the outer envelope may contain regulated ion channels (Cline et al, 1981;Block et al, 1983;Douce and Joyard, 1990;Pohlmeyer et al, 1998;Flugge, 2000;Bolter and Soll, 2001). Thus, we consider it likely that AtPEM candidates represent the majority of integral plastid envelope proteins.…”

Section: Plastid Envelope Membrane Protein Candidatesmentioning

confidence: 99%

The Predicted Candidates of Arabidopsis Plastid Inner Envelope Membrane Proteins and Their Expression Profiles,

Koo

Ohlrogge

2002

Plant Physiology

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Plastid envelope proteins from the Arabidopsis nuclear genome were predicted using computational methods. Selection criteria were: first, to find proteins with NH 2 -terminal plastid-targeting peptides from all annotated open reading frames from Arabidopsis; second, to search for proteins with membrane-spanning domains among the predicted plastidial-targeted proteins; and third, to subtract known thylakoid membrane proteins. Five hundred forty-one proteins were selected as potential candidates of the Arabidopsis plastid inner envelope membrane proteins (AtPEM candidates). Only 34% (183) of the AtPEM candidates could be assigned to putative functions based on sequence similarity to proteins of known function (compared with the 69% function assignment of the total predicted proteins in the genome). Of the 183 candidates with assigned functions, 40% were classified in the category of "transport facilitation," indicating that this collection is highly enriched in membrane transporters. Information on the predicted proteins, tissue expression data from expressed sequence tags and microarrays, and publicly available T-DNA insertion lines were collected. The data set complements proteomic-based efforts in the increased detection of integral membrane proteins, low-abundance proteins, or those not expressed in tissues selected for proteomic analysis. Digital northern analysis of expressed sequence tags suggested that the transcript levels of most AtPEM candidates were relatively constant among different tissues in contrast to stroma and the thylakoid proteins. However, both digital northern and microarray analyses identified a number of AtPEM candidates with tissue-specific expression patterns.Plastids exist in a wide range of differential forms, including proplastids, chloroplasts, etioplasts, amyloplasts, leucoplasts, and chromoplasts, depending on the developmental stage and function of the plant cells in which they reside. To a large extent, the types of plastids that are carried by cells determine the metabolic function and products of the particular plant tissue (Kirk and Tilney-Bassett, 1978).One constant feature among the various types of plastids is the double membrane envelope structure that surrounds the organelle. The envelope, especially the inner envelope, effectively separates plastid metabolism from that of the cytosol. At the same time, almost all carbon and a major flux of other metabolites, various polypeptides, and signals must move through the envelope to coordinate and integrate metabolism with the entire cell. Plastid envelopes contain protein transport machinery (Schnell, 1995;Cline and Henry, 1996;Heins et al., 1998), and are a major site for membrane biogenesis. Metabolite transporters from chloroplast and/or nongreen plastids accommodate the requirements of the different photosynthetic or heterotrophic tissues (Kammerer et al., 1998;Neuhaus and Emes, 2000). Membrane constituents (glycerolipids, pigments, and prenylquinones) are synthesized on the envelope membrane as well as the porphyrin ring ...

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Preparation and Characterization of Membrane Fractions Enriched in Outer and Inner Envelope Membranes from Spinach Chloroplasts

Cited by 171 publications

References 10 publications

Chloroplast Biogenesis. Regulation of Lipid Transport to the Thylakoid in Chloroplasts Isolated from Expanding and Fully Expanded Leaves of Pea

Chloroplast Biogenesis. Regulation of Lipid Transport to the Thylakoid in Chloroplasts Isolated from Expanding and Fully Expanded Leaves of Pea

Glycerolipid transfer for the building of membranes in plant cells

The Predicted Candidates of Arabidopsis Plastid Inner Envelope Membrane Proteins and Their Expression Profiles,

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