Glycolate oxidase isoforms are distributed between the bundle sheath and mesophyll tissues of maize leaves

Popov, Vasily N.; Dmitrieva, Elena; Епринцев, А. Т.; Igamberdiev, Abir U.

doi:10.1078/0176-1617-01105

Cited by 21 publications

(11 citation statements)

References 30 publications

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“…Two isoforms are localized to the BS, representing 80% of the total activity, and one to the M cells (Popov et al, 2003). Given the restriction of Rubisco to the BS cells, it is perhaps not surprising that the majority of the GO activity is restricted to this compartment.…”

Section: Discussionmentioning

confidence: 99%

High Glycolate Oxidase Activity Is Required for Survival of Maize in Normal Air

et al. 2008

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A mutant in the maize (Zea mays) Glycolate Oxidase1 (GO1) gene was characterized to investigate the role of photorespiration in C4 photosynthesis. An Activator-induced allele of GO1 conditioned a seedling lethal phenotype when homozygous and had 5% to 10% of wild-type GO activity. Growth of seedlings in high CO2 (1%-5%) was sufficient to rescue the mutant phenotype. Upon transfer to normal air, the go1 mutant became necrotic within 7 d and plants died within 15 d. Providing [1-14C]glycolate to leaf tissue of go1 mutants in darkness confirmed that the substrate is inefficiently converted to 14CO2, but both wild-type and GO-deficient mutant seedlings metabolized [1-14C]glycine similarly to produce [14C]serine and 14CO2 in a 1:1 ratio, suggesting that the photorespiratory pathway is otherwise normal in the mutant. The net CO2 assimilation rate in wild-type leaves was only slightly inhibited in 50% O2 in high light but decreased rapidly and linearly with time in leaves with low GO. When go1 mutants were shifted from high CO2 to air in light, they accumulated glycolate linearly for 6 h to levels 7-fold higher than wild type and 11-fold higher after 25 h. These studies show that C4 photosynthesis in maize is dependent on photorespiration throughout seedling development and support the view that the carbon oxidation pathway evolved to prevent accumulation of toxic glycolate.

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Section: Discussionmentioning

confidence: 99%

High Glycolate Oxidase Activity Is Required for Survival of Maize in Normal Air

et al. 2008

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“…In C 4 plants, Rubisco and glycolate-2-P phosphatase also occur in the BS cells, together with the glycine oxidation system, whereas glycerate kinase is localized in the M cells (Usuda and Edwards 1980;Leegood 1997). The peroxisomal enzymes of the glycolate pathway are distributed in both cell types, but unevenly (Ohnishi and Kanai 1985;Popov et al 2003). Thus, the intercellular movement of photorespiratory metabolites is complex in C 4 plants.…”

Section: Structural Characterization Of the Bs Cells In C 3 Speciesmentioning

confidence: 96%

Structural and biochemical bases of photorespiration in C4 plants: quantification of organelles and glycine decarboxylase

Yoshimura

Kubota

Ueno

2004

Planta

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In C(4) plants, photorespiration is decreased relative to C(3) plants. However, it remains unclear how much photorespiratory capacity C(4) leaf tissues actually have. We thoroughly investigated the quantitative distribution of photorespiratory organelles and the immunogold localization of the P protein of glycine decarboxylase (GDC) in mesophyll (M) and bundle sheath (BS) cells of various C(4) grass species. Specific differences occurred in the proportions of mitochondria and peroxisomes in the BS cells (relative to the M cells) in photosynthetic tissues surrounding a vein: lower in the NADP-malic enzyme (NADP-ME) species having poorly formed grana in the BS chloroplasts, and higher in the NAD-malic enzyme (NAD-ME) and phosphoenolpyruvate carboxykinase (PCK) species having well developed grana. In all C(4) species, GDC was localized mainly in the BS mitochondria. When the total amounts of GDC in the BS mitochondria per unit leaf width were estimated from the immunogold labeling density and the quantity of mitochondria, the BSs of NADP-ME species contained less GDC than those of NAD-ME or PCK species. This trend was also verified by immunoblot analysis of leaf soluble protein. There was a high positive correlation between the degree of granal development (granal index) in the BS chloroplasts and the total amount of GDC in the BS mitochondria. The variations in the structural and biochemical features involved in photorespiration found among C(4) species might reflect differences in the O(2)/CO(2) partial pressure and in the potential photorespiratory capacity of the BS cells.

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“…Interestingly, previous studies have shown differences between the kinetic parameters of GOXs from C 3 and C 4 plant species. GOX from C 4 species appear to have a lower K m for glycolate (10 M for Amaranthus hypochondriacus and 23 and 65 M for Zea mays guard cells and mesophyll cells, respectively) compared with C 3 species (330 M for Cucurbita pepo cotyledons, 300 M for Pisum sativum, 1 mM for S. oleracea, and 1.9 mM for Arabidopsis thaliana GOX2) (13)(14)(15)(16). These obser-FIGURE 1.…”

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confidence: 88%

Experimental Evidence for a Hydride Transfer Mechanism in Plant Glycolate Oxidase Catalysis

Dellero

Mauve

Boex-Fontvieille

et al. 2015

Journal of Biological Chemistry

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Background: Uncertainty remains about the nature of transition states along the reductive half-reaction of glycolate oxidase. Results: Deuterated glycolate and solvent slow down plant glycolate oxidase catalysis to a modest extent. Conclusion: Isotope effects support a hydride transfer mechanism and indicate glycolate deprotonation to be only partially rate-limiting. Significance: Understanding the catalytic mechanism of the enzyme is crucial for designing drugs/herbicides to inhibit its activity.

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Glycolate oxidase isoforms are distributed between the bundle sheath and mesophyll tissues of maize leaves

Cited by 21 publications

References 30 publications

High Glycolate Oxidase Activity Is Required for Survival of Maize in Normal Air

High Glycolate Oxidase Activity Is Required for Survival of Maize in Normal Air

Structural and biochemical bases of photorespiration in C4 plants: quantification of organelles and glycine decarboxylase

Experimental Evidence for a Hydride Transfer Mechanism in Plant Glycolate Oxidase Catalysis

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