Localization of glycolate dehydrogenase in two species of Dunaliella

Stabenau, H.; Winkler, U.; Säftel, W.

doi:10.1007/bf00195694

Cited by 19 publications

(12 citation statements)

References 13 publications

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“…We also considered another way to detect microbodies using immunoelectron microscopy or immunofluorescent microscopy analysis, but no antibody that specifically reacts with microbodies or specific molecular probes for microbodies of Chlamydomonas reinhardtii are currently available. Even catalase, which is a normal marker of peroxisomes, is not found in the peroxisomes of Chlamydomonas reinhardtii cells (Kato et al 1997), and existing emzymes in the peroxisomes of Chlamydomonas cells cannot be revealed because we do not know the role of peroxisomes in Chlamydomonas (Stabenau et al 1993). Since many unresolved issues persist for study of peroxisomes in Chlamydomonas, we believe that visualization of microbodies in Chlamydomonas cells might be a good way to initiate future study on peroxisomes in Chlamydomonas.…”

Section: Discussionmentioning

confidence: 96%

“…In Chlorophyceae and Ulvophyceae, except Charophyceae, mitochondria have enzymes of glycolate metabolism (Frederick et al 1973), and glycolate is metabolized by mitochondrial glycolate dehydrogenase. In both Dunaliella and Eremosphaera (Chlorophyceae), microbodies contain catalase, uricase (Stabenau 1984) and hydroxyacyl-CoA dehydrogenase, while glycolate dehydrogenase and hydroxypyruvate reductase are located in mitochondria (Stabenau et al 1993). In C. reinhardtii, catalase is found in the mitochondria (Kato et al 1997).…”

Section: Discussionmentioning

confidence: 98%

“…On the other hand, microbodies in some green algae (e.g., Dunaliella and Etemosphaera: both of Chlorophyceae) contain fewer enzymes than the peroxisomes of higher plants (Stabenau 1974a(Stabenau , b, 1984Stabenau et al 1993). Nowadays, it is common knowledge that microbodies in Chlorophyceae are similar to unspecialized peroxisomes of higher plants.…”

Section: Introductionmentioning

confidence: 96%

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Visualization of microbodies in Chlamydomonas reinhardtii

Hayashi

Shinozaki

2011

J Plant Res

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In Chlorophycean algal cells, these organelles are generally called microbodies because they lack the enzymes found in the peroxisomes of higher plants. Microbodies in some algae contain fewer enzymes than the peroxisomes of higher plants, and some unicellular green algae in Chlorophyceae such as Chlamydomonas reinhardtii do not possess catalase, an enzyme commonly found in peroxisomes. Thus, whether microbodies in Chlorophycean algae are similar to the peroxisomes of higher plants, and whether they use a similar transport mechanism for the peroxisomal targeting signal (PTS), remain unclear. To determine whether the PTS is present in the microbodies of Chlorophycean algae, and to visualize the microbodies in Chlamydomonas cells, we examined the sub-cellular localization of green fluorescent proteins (GFP) fused to several PTS-like sequences. We detected GFP compartments that were spherical with a diameter of 0.3-1.0 μm in transgenic Chlamydomonas. Comparative analysis of the character of GFP-compartments observed by fluorescence microscopy and that of microbodies by electron microscopy indicated that the compartments were one and the same. The result also showed that the microbodies in Chlorophycean cells have a similar transport mechanism to that of peroxisomes of higher plants.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 96%

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Visualization of microbodies in Chlamydomonas reinhardtii

Hayashi

Shinozaki

2011

J Plant Res

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“…According to our present knowledge it seems likely that Chlorophyta and Charophyta evolved from a common ancestor which was among prasinophyte‐like scaly flagellates. Probably, the mitochondrial glycolate pathway was already present in this ancestor, because glycolate dehydrogenase but not glycolate oxidase can be demonstrated in procaryotes (Husic and Tolbert 1992) as well as in very primitive prasinophycean algae (Stabenau et al 1989, 1993). Apparently, the more effective peroxisomal glycolate pathway was acquired during the development of Charophyceae and it is very interesting that the basic mitochondrial pathway or parts of it may still be conserved even in land plants like Arabidopsis (Bari et al 2004).…”

Section: Discussionmentioning

confidence: 99%

Glycolate metabolism in green algae

Stabenau

Winkler

2005

Physiologia Plantarum

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Using 14C‐labelled substrates, the succession of the single steps in the glycolate metabolism was investigated in Mougeotia scalaris and Eremosphaera viridis, which, within the group of green algae, are representatives of the evolutionary lines of Charophyta and Chlorophyta, respectively. In both algae the same metabolites are formed as in higher plants, although in Eremosphaera, which in contrast to Mougeotia does not possess leaf peroxisomes, all reactions are exclusively mitochondrial. Concomitant with the oxidation of glycolate, the synthesis of ATP was demonstrated in Eremosphaera. Formation of tartronic semi‐aldehyde or other products different from those in land plants could not be demonstrated in either of these algae. Excretion of glycolate by Mougeotia and Eremosphaera is enhanced by decreasing the CO2 concentration as well as by increasing the light intensity, but is completely stopped about 14 h later. Whereas increasing enzyme activities of the glycolate pathway apparently reduces glycolate excretion in Mougeotia, activation of CO2 pumps seems to be the dominant reaction to prevent glycolate excretion in Eremosphaera. Mesostigma viride is one of the phylogenetically oldest algae in the group of Charophyceae. As this alga has already been demonstrated to contain microbodies with enzymes of leaf peroxisomes, the peroxisomal glycolate pathway must have originated at a very early stage. Surprisingly, the organelles from Mesostigma contain also the glyoxysomal marker enzyme isocitrate lyase suggesting these microbodies to be prototypes from which both glyoxysomes and leaf peroxisomes evolved.

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“…Moreover, the compartmentalisation of photorespiratory enzymes appears to be only partially conserved in algae, as some enzymes of 2PG metabolism, including catalase, are located within the mitochondria in green algae (Stabenau et al . , ; Kato et al . ).…”

Section: Impact Of Peroxisome Specialisation On Photorespirationmentioning

confidence: 99%

Evolution of the biochemistry of the photorespiratory C2 cycle

et al. 2012

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Oxygenic photosynthesis would not be possible without photorespiration in the present day O2 -rich atmosphere. It is now generally accepted that cyanobacteria-like prokaryotes first evolved oxygenic photosynthesis, which was later conveyed via endosymbiosis into a eukaryotic host, which then gave rise to the different groups of algae and streptophytes. For photosynthetic CO2 fixation, all these organisms use RubisCO, which catalyses both the carboxylation and the oxygenation of ribulose 1,5-bisphosphate. One of the reaction products of the oxygenase reaction, 2-phosphoglycolate (2PG), represents the starting point of the photorespiratory C2 cycle, which is considered largely responsible for recapturing organic carbon via conversion to the Calvin-Benson cycle (CBC) intermediate 3-phosphoglycerate, thereby detoxifying critical intermediates. Here we discuss possible scenarios for the evolution of this process toward the well-defined 2PG metabolism in extant plants. While the origin of the C2 cycle core enzymes can be clearly dated back towards the different endosymbiotic events, the evolutionary scenario that allowed the compartmentalised high flux photorespiratory cycle is uncertain, but probably occurred early during the algal radiation. The change in atmospheric CO2 /O2 ratios promoting the acquisition of different modes for inorganic carbon concentration mechanisms, as well as the evolutionary specialisation of peroxisomes, clearly had a dramatic impact on further aspects of land plant photorespiration.

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Localization of glycolate dehydrogenase in two species of Dunaliella

Cited by 19 publications

References 13 publications

Visualization of microbodies in Chlamydomonas reinhardtii

Visualization of microbodies in Chlamydomonas reinhardtii

Glycolate metabolism in green algae

Evolution of the biochemistry of the photorespiratory C2 cycle

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