Peroxisomes and their Assembly in Higher Plants

Olsen, and L J; Harada, John J.

doi:10.1146/annurev.pp.46.060195.001011

Cited by 80 publications

(44 citation statements)

References 111 publications

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“…During photomorphogenesis, as seedlings undergo the transition from heterotrophic to autotrophic growth, organelles involved in photosynthesis and related functions (such as photorespiration) need to develop and genes required in these processes need to be activated. It was suggested that, during such a transitional stage, glyoxysomes are converted into leaf peroxisomes by replacement of glyoxysome-specific enzymes with those characteristic of leaf-type peroxisomes (Trelease et al, 1971;Olsen and Harada, 1995). In this study, we observed in Arabidopsis seedlings peroxisome elongation after 0.5-h light exposure, constriction and fission of these organelles at 2 h, and a sheer increase in peroxisome abundance at 4 and 8 h (Fig.…”

Section: Discussionsupporting

confidence: 52%

“…Plant peroxisomes can be categorized into several variants that are structurally similar but metabolically distinct, such as glyoxysomes in seeds and germinating seedlings, leaf peroxisomes, glyoxysome-related gerontosomes in senescent tissue, nodule-specific peroxisomes, and unspecialized peroxisomes. Functions attributed to plant peroxisomes include metabolism of lipids, reactive oxygen species, and nitrogen, photorespiration, plant hormone biosynthesis and metabolism, and plant pathogen interaction (Beevers, 1979;Olsen and Harada, 1995;Zolman et al, 2000;Hayashi and Nishimura, 2003;Lipka et al, 2005;McCartney et al, 2005;Nyathi and Baker, 2006;Reumann and Weber, 2006).…”

mentioning

confidence: 99%

“…When exposed to light, Arabidopsis seedlings undergo a process called photomorphogenesis, in which cotyledons open, hypocotyl growth is inhibited, chloroplasts develop, and genes involved in photosynthesis and related functions are activated (Wang and Deng, 2002a). During this process, glyoxysomes are converted into leaf peroxisomes by replacing enzymes specific for lipid metabolism during germination with proteins involved in the glycolate recycling during photorespiration (Olsen and Harada, 1995). Previously, we identified a gain-of-function mutation in a peroxisomal gene (PEX2) in Arabidopsis that partially suppressed the photomorphogenic (deetiolated) phenotype of the mutant defective in the nuclear protein DET1 (Hu et al, 2002).…”

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Light Induces Peroxisome Proliferation in Arabidopsis Seedlings through the Photoreceptor Phytochrome A, the Transcription Factor HY5 HOMOLOG, and the Peroxisomal Protein PEROXIN11b

Desai

2008

Plant Physiology

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Peroxisomes are single membrane-delimited subcellular organelles that carry out numerous vital metabolic reactions in nearly all eukaryotes. Peroxisomes alter their morphology, abundance, and enzymatic constituents in response to environmental cues, yet little is known about the underlying mechanisms. In this work, we investigated the regulatory role of light in peroxisome proliferation in Arabidopsis (Arabidopsis thaliana). We provide evidence that light induces proliferation of peroxisomes in Arabidopsis seedlings and that the peroxisomal protein PEX11b plays an important role in mediating this process. The far-red light receptor phytochrome A (phyA) and the bZIP transcription factor HY5 HOMOLOG (HYH) are both required for the up-regulation of PEX11b in the light. We further demonstrate that the phyA and hyh mutants exhibit reduced peroxisome abundance, a phenotype that can be rescued by overexpressing PEX11b in these plants. The HYH protein is able to bind to the promoter of PEX11b, suggesting that the PEX11b gene is a direct target of HYH. We conclude that HYH and PEX11b constitute a novel branch of the phyA-mediated light signaling cascade, which promotes peroxisome proliferation during seedling photomorphogenesis.

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Section: Discussionsupporting

confidence: 52%

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confidence: 99%

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confidence: 99%

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Light Induces Peroxisome Proliferation in Arabidopsis Seedlings through the Photoreceptor Phytochrome A, the Transcription Factor HY5 HOMOLOG, and the Peroxisomal Protein PEROXIN11b

Desai

2008

Plant Physiology

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“…Glyoxysomes are a class of higher plant peroxisomes containing enzymes unique to reactions of the glyoxylate cycle and P-oxidation of fatty acids (Olsen and Harada, 1995;Gietl, 1996). Cotyledons of most plants contain glyoxysomes that are involved in lipid mobilization to provide nutrients during germination and seedling growth.…”

mentioning

confidence: 99%

“…Cotyledons of most plants contain glyoxysomes that are involved in lipid mobilization to provide nutrients during germination and seedling growth. Leaves, roots, and mature pollen each possess a distinct class of peroxisomes, each performing physiological functions specific to the tissue (Olsen and Harada, 1995;Gietl, 1996). However, a11 peroxisomes contain catalase and other hydrogen peroxide-metabolizing enzymes and are bound by a single membrane.…”

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Protein Transport into Higher Plant Peroxisomes (In Vitro Import Assay Provides Evidence for Receptor Involvement)

1997

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Peroxisome biogenesis requires that proteins be transported from their site of synthesis in the cytoplasm to their final location in the peroxisome matrix or membrane. Glyoxysomes are a class of peroxisomes found primarily in germinating seedlings and are involved in mobilizing fatty acids via the glyoxylate cycle and the p-oxidation pathway. We have used an in vitro assay to study the mechanism(s) of import of proteins into glyoxysomes. Results from this assay indicate that the transport process i s time-and temperaturedependent and is specific for peroxisomal proteins. lsocitrate lyase, a glyoxysomal protein, and the leaf-type peroxisomal enzyme glycolate oxidase (CLO) were transported into pumpkin (Cucurbita pepo) glyoxysomes with no apparent differences in efficiency of import. Thus, this in vitro assay appears to be physiologically relevant and correlates well with expected in vivo conditions. Protein import was also energy-dependent and saturable. Nonradiolabeled

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Isolation of Glyoxysomes from Pumpkin Cotyledons

Harrison-Lowe

Olsen

2005

CP Cell Biology

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Peroxisomes are single‐membrane‐bound organelles found in virtually all eukaryotes. In plants, there are several classes of peroxisomes. Glyoxysomes are found in germinating seedlings and contain enzymes specific for the glyoxylate cycle, including isocitrate lyase and malate synthase. After seedlings become photosynthetic, leaf peroxisomes participate in reactions of the photorespiration pathway and contain characteristic enzymes such as glycolate oxidase and hydroxypyruvate reductase. As leaves begin to senesce, leaf peroxisomes are transformed back into glyoxysomes. Root peroxisomes in the nodules of legumes, for example, sequester enzymes such as allantoinase and uricase, which contribute to nitrogen metabolism in these tissues. Thus, peroxisomes participate in many metabolic pathways and contain specific enzyme complements, depending on the tissue source. All peroxisomes contain catalase to degrade hydrogen peroxide and enzymes to accomplish β‐oxidation of fatty acids. Glyoxysomes can be isolated from pumpkin cotyledons by standard differential centrifugation and density separation, as described in this article.

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Peroxisomes and their Assembly in Higher Plants

Cited by 80 publications

References 111 publications

Light Induces Peroxisome Proliferation in Arabidopsis Seedlings through the Photoreceptor Phytochrome A, the Transcription Factor HY5 HOMOLOG, and the Peroxisomal Protein PEROXIN11b

Light Induces Peroxisome Proliferation in Arabidopsis Seedlings through the Photoreceptor Phytochrome A, the Transcription Factor HY5 HOMOLOG, and the Peroxisomal Protein PEROXIN11b

Protein Transport into Higher Plant Peroxisomes (In Vitro Import Assay Provides Evidence for Receptor Involvement)

Isolation of Glyoxysomes from Pumpkin Cotyledons

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