The evolution of eukaryotic cells from the perspective of peroxisomes

Bolte, Kathrin; Rensing, Stefan A.; Maier, Uwe‐G.

doi:10.1002/bies.201400151

Cited by 47 publications

(24 citation statements)

References 67 publications

(98 reference statements)

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“…These structures are small, membrane-enclosed organelles, discovered by Christian De Duve (De Duve, 1969) that employ enzymes involved in a variety of energetic and metabolic reactions (Speijer (2011) BioEssays 33:88; Bolte et al (2015) BioEssays 37:195; Moore (2015) BioEssays 37:113). De Duve hypothesized that peroxisomes originated due to endoplasmic reticulum (ER) stress caused by rising levels of oxygen in the environment (Berner et al, 2000).…”

Section: Physical Phenomena and Cellular Requirementsmentioning

confidence: 99%

The resolution of ambiguity as the basis for life: A cellular bridge between Western reductionism and Eastern holism

Torday

Miller

2017

Progress in Biophysics and Molecular Biology

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Boundary conditions enable cellular life through negentropy, chemiosmosis, and homeostasis as identifiable First Principles of Physiology. Self-referential awareness of status arises from this organized state to sustain homeostatic imperatives. Preferred homeostatic status is dependent upon the appraisal of information and its communication. However, among living entities, sources of information and their dissemination are always imprecise. Consequently, living systems exist within an innate state of ambiguity. It is presented that cellular life and evolutionary development are a self-organizing cellular response to uncertainty in iterative conformity with its basal initiating parameters. Viewing the life circumstance in this manner permits a reasoned unification between Western rational reductionism and Eastern holism.

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Section: Physical Phenomena and Cellular Requirementsmentioning

confidence: 99%

The resolution of ambiguity as the basis for life: A cellular bridge between Western reductionism and Eastern holism

Torday

Miller

2017

Progress in Biophysics and Molecular Biology

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“…This bypasses the respiratory chain, leading to loss of ATP generation from FADH 2 oxidation and H 2 O 2 formation. Interestingly, it was recently found that all peroxisomal enzymes involved (two enzymes, as steps 2 and 3 are catalysed by a single bifunctional enzyme after gene fusion), of course apart from the peroxisomal acyl-CoA oxidase used in step 1, are derived from mitochondria [41]. Though ‘peroxisomes’ now have accreted many extra functions (differing per species and tissue), comparative analysis shows β-oxidation to be their most ancient pathway [27,41].…”

Section: Peroxisomesmentioning

confidence: 99%

“…Interestingly, it was recently found that all peroxisomal enzymes involved (two enzymes, as steps 2 and 3 are catalysed by a single bifunctional enzyme after gene fusion), of course apart from the peroxisomal acyl-CoA oxidase used in step 1, are derived from mitochondria [41]. Though ‘peroxisomes’ now have accreted many extra functions (differing per species and tissue), comparative analysis shows β-oxidation to be their most ancient pathway [27,41]. More complicated pathways are presumed to have been relocated in eukaryotes, maybe following positive selection of low levels of proteins ending up in aberrant cellular environments [42].…”

Section: Peroxisomesmentioning

confidence: 99%

Being right on Q: shaping eukaryotic evolution

Speijer

2016

Biochemical Journal

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Reactive oxygen species (ROS) formation by mitochondria is an incompletely understood eukaryotic process. I proposed a kinetic model [BioEssays (2011) 33, 88–94] in which the ratio between electrons entering the respiratory chain via FADH2 or NADH (the F/N ratio) is a crucial determinant of ROS formation. During glucose breakdown, the ratio is low, while during fatty acid breakdown, the ratio is high (the longer the fatty acid, the higher is the ratio), leading to higher ROS levels. Thus, breakdown of (very-long-chain) fatty acids should occur without generating extra FADH2 in mitochondria. This explains peroxisome evolution. A potential ROS increase could also explain the absence of fatty acid oxidation in long-lived cells (neurons) as well as other eukaryotic adaptations, such as dynamic supercomplex formation. Effective combinations of metabolic pathways from the host and the endosymbiont (mitochondrion) allowed larger varieties of substrates (with different F/N ratios) to be oxidized, but high F/N ratios increase ROS formation. This might have led to carnitine shuttles, uncoupling proteins, and multiple antioxidant mechanisms, especially linked to fatty acid oxidation [BioEssays (2014) 36, 634–643]. Recent data regarding peroxisome evolution and their relationships with mitochondria, ROS formation by Complex I during ischaemia/reperfusion injury, and supercomplex formation adjustment to F/N ratios strongly support the model. I will further discuss the model in the light of experimental findings regarding mitochondrial ROS formation.

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“…The peroxisomal b-oxidation pathway plays an indispensable role in the catabolism of fatty acids in animals, fungi and plants (Bolte et al, 2015). In addition, in plants and animals, b-oxidation in peroxisomes is involved in the metabolism of a number of other specialized compounds (Poirier et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

A peroxisomal thioesterase plays auxiliary roles in plant β‐oxidative benzoic acid metabolism

et al. 2018

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Peroxisomal β-oxidative degradation of compounds is a common metabolic process in eukaryotes. Reported benzoyl-coenzyme A (BA-CoA) thioesterase activity in peroxisomes from petunia flowers suggests that, like mammals and fungi, plants contain auxiliary enzymes mediating β-oxidation. Here we report the identification of Petunia hybrida thioesterase 1 (PhTE1), which catalyzes the hydrolysis of aromatic acyl-CoAs to their corresponding acids in peroxisomes. PhTE1 expression is spatially, developmentally and temporally regulated and exhibits a similar pattern to known benzenoid metabolic genes. PhTE1 activity is inhibited by free coenzyme A (CoA), indicating that PhTE1 is regulated by the peroxisomal CoA pool. PhTE1 downregulation in petunia flowers led to accumulation of BA-CoA with increased production of benzylbenzoate and phenylethylbenzoate, two compounds which rely on the presence of BA-CoA precursor in the cytoplasm, suggesting that acyl-CoAs can be exported from peroxisomes. Furthermore, PhTE1 downregulation resulted in increased pools of cytoplasmic phenylpropanoid pathway intermediates, volatile phenylpropenes, lignin and anthocyanins. These results indicate that PhTE1 influences (i) intraperoxisomal acyl-CoA/CoA levels needed to carry out β-oxidation, (ii) efflux of β-oxidative products, acyl-CoAs and free acids, from peroxisomes, and (iii) flux distribution within the benzenoid/phenylpropanoid metabolic network. Thus, this demonstrates that plant thioesterases play multiple auxiliary roles in peroxisomal β-oxidative metabolism.

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The evolution of eukaryotic cells from the perspective of peroxisomes

Cited by 47 publications

References 67 publications

The resolution of ambiguity as the basis for life: A cellular bridge between Western reductionism and Eastern holism

The resolution of ambiguity as the basis for life: A cellular bridge between Western reductionism and Eastern holism

Being right on Q: shaping eukaryotic evolution

A peroxisomal thioesterase plays auxiliary roles in plant β‐oxidative benzoic acid metabolism

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