Plant peroxisomes: recent discoveries in functional complexity, organelle homeostasis, and morphological dynamics

Reumann, Sigrun; Bartel, Bonnie

doi:10.1016/j.pbi.2016.07.008

Cited by 87 publications

(69 citation statements)

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“…Antioxidant catalase and H 2 O 2 -producing flavin oxidases are essential enzymatic components of these organelles. However, it is surprising to note that their biochemical composition can change depending on the organism, organ type, development stage and environment involved [25], [44], [53], [88], [97], [106], [112], [113].…”

Section: Introductionmentioning

confidence: 99%

Plant peroxisomes: A nitro-oxidative cocktail

et al. 2017

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Although peroxisomes are very simple organelles, research on different species has provided us with an understanding of their importance in terms of cell viability. In addition to the significant role played by plant peroxisomes in the metabolism of reactive oxygen species (ROS), data gathered over the last two decades show that these organelles are an endogenous source of nitric oxide (NO) and related molecules called reactive nitrogen species (RNS). Molecules such as NO and H2O2 act as retrograde signals among the different cellular compartments, thus facilitating integral cellular adaptation to physiological and environmental changes. However, under nitro-oxidative conditions, part of this network can be overloaded, possibly leading to cellular damage and even cell death. This review aims to update our knowledge of the ROS/RNS metabolism, whose important role in plant peroxisomes is still underestimated. However, this pioneering approach, in which key elements such as β-oxidation, superoxide dismutase (SOD) and NO have been mainly described in relation to plant peroxisomes, could also be used to explore peroxisomes from other organisms.

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Section: Introductionmentioning

confidence: 99%

Plant peroxisomes: A nitro-oxidative cocktail

et al. 2017

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“…Our etiolated ubiquitylome datasets also contained numerous peroxisome proteins (26 total) (Figure 4A), including three acyl-CoA oxidases (ACX1 ACX2, and ACX6), acyl-activating enzyme (AAE1), acetylaceto-CoA thiolase (ACAT2), fatty acid reductase (FAR1) and long-chain acyl-CoA synthase required for fatty acid β-oxidation, isocitrate lyase (ICL), peroxisomal citrate synthase (CSY2), and PEX7 and PEX16 required for peroxisomal biogenesis (Reumann and Bartel, 2016). Presumably, some of this ubiquitylation reflects peroxisome breakdown through Ub-mediated autophagy as germinating Arabidopsis cotyledons transition away from using stored lipids for nutrition.…”

Section: Resultsmentioning

confidence: 99%

Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in Remodeling the Arabidopsis Proteome during Photomorphogenesis

et al. 2017

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The switch from skotomorphogenesis to photomorphogenesis is a key developmental transition in the life of seed plants. While much of the underpinning proteome remodeling is driven by light-induced changes in gene expression, the proteolytic removal of specific proteins by the ubiquitin-26S proteasome system is also likely paramount. Through mass spectrometric analysis of ubiquitylated proteins affinity-purified from etiolated Arabidopsis seedlings before and after red-light irradiation, we identified a number of influential proteins whose ubiquitylation status is modified during this switch. We observed a substantial enrichment for proteins involved in auxin, abscisic acid, ethylene, and brassinosteroid signaling, peroxisome function, disease resistance, protein phosphorylation and light perception, including the phytochrome (Phy) A and phototropin photoreceptors. Soon after red-light treatment, PhyA becomes the dominant ubiquitylated species, with ubiquitin attachment sites mapped to six lysines. A PhyA mutant protected from ubiquitin addition at these sites is substantially more stable in planta upon photoconversion to Pfr and is hyperactive in driving photomorphogenesis. However, light still stimulates ubiquitylation and degradation of this mutant, implying that other attachment sites and/or proteolytic pathways exist. Collectively, we expand the catalog of ubiquitylation targets in Arabidopsis and show that this post-translational modification is central to the rewiring of plants for photoautotrophic growth.

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“…In addition to the core processes of b-oxidation and ROS detoxification, plant peroxisomes house diverse specialized functions (for review, see Reumann and Bartel, 2016) that may change during development (Titus and Becker, 1985;Nishimura et al, 1986;Sautter, 1986; or in response to environmental cues (for review, see Goto-Yamada et al, 2015). For example, plant peroxisomes sequester enzymes acting in photorespiration, which is important when ribulose-1,5-bisphosphate carboxylase/oxygenase fixes O 2 instead of CO 2 .…”

Section: Photorespiration: Not Just For Chloroplastsmentioning

confidence: 99%

“…When b-oxidation is slowed, as in pxa1, sdp1, or cgi-58 mutants, stomatal opening is impeded (McLachlan et al, 2016). Because environmental stimuli, such as light and temperature, regulate stomatal aperture to control water and gas exchange (for review, Peroxisomes house a variety of catabolic and biosynthetic reactions (Reumann and Bartel, 2016), several of which generate H 2 O 2 and other ROS (orange). b-oxidation (red) is used to catabolize fatty acids (purple) and in the synthesis of several hormones (blue).…”

mentioning

confidence: 99%