Etioplast Differentiation in Arabidopsis: Both PORA and PORB Restore the Prolamellar Body and Photoactive Protochlorophyllide–F655 to the <i>cop1</i> Photomorphogenic Mutant

Sperling, Ulrich; Franck, Fabrice; Cleve, Barbara van; Frick, Geneviève; Apel, Klaus; Armstrong, Gregory A.

doi:10.1105/tpc.10.2.283

Cited by 112 publications

(140 citation statements)

References 55 publications

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“…A positive band of Chlide a was found at 688 nm as the result of photoactive Pchlide a transformation (negative band at 655 nm). The obtained difference spectrum was similar to the difference spectra obtained in angiosperms (Sperling et al, 1998). To visualize rapid Pchlide a and Chlide a shifts in darkness after one flash, we calculated difference spectra between samples frozen 30 s and immediately after one flash (30-s darknessminus-flash, Fig 7, curve b).…”

Section: Photoreduction and Regeneration Of Photoactive Pchlide A Trimentioning

confidence: 81%

“…The ability to synthesize Chl in darkness is linked to the presence of three genes (chlL, chlN, and chlB) in the chloroplast genome coding for subunits of the light-independent Pchlide reductase (for review, see Armstrong, 1998). At least two of these genes are absent from the angiosperm chloroplast genome, which consequently are unable to synthesize Chl in darkness (Shimada and Sugiura, 1991;Suzuki and Bauer, 1992).…”

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confidence: 99%

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Chlorophyll Synthesis in Dark-Grown Pine Primary Needles

Schoefs

Franck

1998

Plant Physiology

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The pigment content of dark-grown primary needles of Pinus jeffreyi L. and Pinus sylvestris L. was determined by highperformance liquid chromatography. The state of protochlorophyllide a and of chlorophylls during dark growth were analyzed by in situ 77 K fluorescence spectroscopy. Both measurements unambiguously demonstrated that pine primary needles are able to synthesize chlorophyll in the dark. Norflurazon strongly inhibited both carotenoid and chlorophyll synthesis. Needles of plants treated with this inhibitor had low chlorophyll content, contained only traces of xanthophylls, and accumulated carotenoid precursors. The first form of chlorophyll detected in young pine needles grown in darkness had an emission maximum at 678 nm. Chlorophyll-protein complexes with in situ spectroscopic properties similar to those of fully green needles (685, 695, and 735 nm) later accumulated in untreated plants, whereas in norflurazon-treated plants the photosystem I emission at 735 nm was completely lacking. To better characterize the light-dependent chlorophyll biosynthetic pathway in pine needles, the 77 K fluorescence properties of in situ protochlorophyllide a spectral forms were studied. Photoactive and nonphotoactive protochlorophyllide a forms with emission properties similar to those reported for dark-grown angiosperms were found, but excitation spectra were substantially red shifted. Because of their lower chlorophyll content, norflurazon-treated plants were used to study the protochlorophyllide a photoreduction process triggered by one light flash. The first stable chlorophyllide photoproduct was a chlorophyllide a form emitting at 688 nm as in angiosperms. Further chlorophyllide a shifts usually observed in angiosperms were not detected. The rapid regeneration of photoactive protochlorophyllide a from nonphotoactive protochlorophyllide after one flash was demonstrated.

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Section: Photoreduction and Regeneration Of Photoactive Pchlide A Trimentioning

confidence: 81%

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confidence: 99%

Chlorophyll Synthesis in Dark-Grown Pine Primary Needles

Schoefs

Franck

1998

Plant Physiology

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“…The SDs calculated from the averages of the independent experiments are indicated. Average values and the number of peptides used for each independent experiment are listed in Supplemental Table II phyllide reductase a/b (band 2), as expected in prolamellar bodies (Sperling et al, 1998), and a mixture of proteins unrelated to PGs in band 1 (Fig. 2B).…”

Section: Purification and Identification Of The Proteome Of Low-densimentioning

confidence: 99%

Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

2006

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Plastoglobules (PGs) are oval or tubular lipid-rich structures present in all plastid types, but their specific functions are unclear. PGs contain quinones, a-tocopherol, and lipids and, in chromoplasts, carotenoids as well. It is not known whether PGs contain any enzymes or regulatory proteins. Here, we determined the proteome of PGs from chloroplasts of stressed and unstressed leaves of Arabidopsis (Arabidopsis thaliana) as well as from pepper (Capsicum annuum) fruit chromoplasts using mass spectrometry. Together, this showed that the proteome of chloroplast PGs consists of seven fibrillins, providing a protein coat and preventing coalescence of the PGs, and an additional 25 proteins likely involved in metabolism of isoprenoid-derived molecules (quinines and tocochromanols), lipids, and carotenoid cleavage. Four unknown ABC1 kinases were identified, possibly involved in regulation of quinone monooxygenases. Most proteins have not been observed earlier but have predicted N-terminal chloroplast transit peptides and lack transmembrane domains, consistent with localization in the PG lipid monolayer particles. Quantitative differences in PG composition in response to high light stress and degreening were determined by differential stable-isotope labeling using formaldehyde. More than 20 proteins were identified in the PG proteome of pepper chromoplasts, including four enzymes of carotenoid biosynthesis and several homologs of proteins observed in the chloroplast PGs. Our data strongly suggest that PGs in chloroplasts form a functional metabolic link between the inner envelope and thylakoid membranes and play a role in breakdown of carotenoids and oxidative stress defense, whereas PGs in chromoplasts are also an active site for carotenoid conversions.

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“…The prolamellar body (PLB) has a lipid composition similar to that of the thylakoids lutein and violaxanthin and the chlorophyll tetrapyrrole precursor protochlorophyllide (Pchlide), which is bound to its enzyme, protochlorophyllide oxidoreductase (POR) (Joyard et al, 1998). Both Pchlide and POR are essential for PLB formation (Nielsen and Gough, 1974;Armstrong et al, 1995;Lebedev et al, 1995;Sundqvist and Dahlin, 1997;Sperling et al, 1998). Upon illumination, the PLB disperses to form thylakoids, photosystems are assembled, and chlorophylls and the full complement of carotenoids are synthesized (Fankhauser and Chory, 1997).…”

Section: Introductionmentioning

confidence: 99%

Identification of the Carotenoid Isomerase Provides Insight into Carotenoid Biosynthesis, Prolamellar Body Formation, and Photomorphogenesis

et al. 2002

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Carotenoids are essential photoprotective and antioxidant pigments synthesized by all photosynthetic organisms. Most carotenoid biosynthetic enzymes were thought to have evolved independently in bacteria and plants. For example, in bacteria, a single enzyme (CrtI) catalyzes the four desaturations leading from the colorless compound phytoene to the red compound lycopene, whereas plants require two desaturases (phytoene and -carotene desaturases) that are unrelated to the bacterial enzyme. We have demonstrated that carotenoid desaturation in plants requires a third distinct enzyme activity, the carotenoid isomerase (CRTISO), which, unlike phytoene and -carotene desaturases, apparently arose from a progenitor bacterial desaturase. The Arabidopsis CRTISO locus was identified by the partial inhibition of lutein synthesis in light-grown tissue and the accumulation of poly-cis -carotene precursors in dark-grown tissue of crtISO mutants. After positional cloning, enzymatic analysis of CRTISO expressed in Escherichia coli confirmed that the enzyme catalyzes the isomerization of poly-cis -carotenoids to all-trans -carotenoids. Etioplasts of darkgrown crtISO mutants accumulate acyclic poly-cis -carotenoids in place of cyclic all-trans -xanthophylls and also lack prolamellar bodies (PLBs), the lattice of tubular membranes that defines an etioplast. This demonstrates a requirement for carotenoid biosynthesis to form the PLB. The absence of PLBs in crtISO mutants demonstrates a function for this unique structure and carotenoids in facilitating chloroplast development during the first critical days of seedling germination and photomorphogenesis.

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Etioplast Differentiation in Arabidopsis: Both PORA and PORB Restore the Prolamellar Body and Photoactive Protochlorophyllide–F655 to the cop1 Photomorphogenic Mutant

Cited by 112 publications

References 55 publications

Chlorophyll Synthesis in Dark-Grown Pine Primary Needles

Chlorophyll Synthesis in Dark-Grown Pine Primary Needles

Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

Identification of the Carotenoid Isomerase Provides Insight into Carotenoid Biosynthesis, Prolamellar Body Formation, and Photomorphogenesis

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