The argentia mutation delays normal development of photosynthetic cell-types in Zea mays

Langdale, Jane A.; Metzler, Mary; Nelson, Timothy

doi:10.1016/0012-1606(87)90349-6

Cited by 74 publications

(73 citation statements)

References 25 publications

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“…NADP-MDH mRNA accumulation is light induced and M cell specific in maize (Sheen and Bogorad, 1987;Metzler et al, 1989) and in sorghum (Crétin et al, 1988). During the development of the maize leaf, the accumulation of NADP-MDH mRNA in M progenitor cells coincides with that for rbcS in BS progenitor cells and occurs early in development before mRNAs of other C, pathway enzymes can be detected (Langdale et al, 1987). Furthermore, NADP-MDH is present in C,-photosynthesizing regions of husk leaves in the absence of other C, enzymes (Langdale et al, 1988).…”

mentioning

confidence: 88%

“…Protein was prepared according to Langdale et al (1987) with the addition of 0.1 mM PMSF to the protein extraction buffer. Protein concentrations were determined using the Bradford Assay (Bio-Rad) (Bradford, 1976).…”

Section: Protein Preparation and Analysismentioning

confidence: 99%

“…Furthermore, NADP-MDH is present in C,-photosynthesizing regions of husk leaves in the absence of other C, enzymes (Langdale et al, 1988). In the slow-greening argentia maize mutant, in which message levels for most C, enzymes are down-regulated, NADP-MDH message levels are comparable to those in wild-type leaves (Langdale et al, 1987). Although the products of the two MDH genes were not distinguished in these studies, these findings suggest a substantial role for NADP-MDH in the default C, photosynthesis that is thought to occur early in maize leaf development or in early organellar metabolism prior to its C, role.…”

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confidence: 94%

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C4 Isoform of NADP-Malate Dehydrogenase (cDNA Cloning and Expression in Leaves of C4, C3, and C3-C4 Intermediate Species of Flaveria)

McGonigle

Nelson

1995

Plant Physiol.

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In C, plants of the NADP-malic enzyme type, an abundant, mesophyll cell-localized NADP-malate dehydrogenase (MDH) acts to convert oxaloacetate, the initial product of carbon fixation, to malate before it is shuttled to the bundle sheath. Since NADP-MDH has different but important roles in leaves of C, and C, plants, we have cloned and characterized a nearly full-length cDNA encoding NADP-MDH from Flaveria trinervia (C,) to permit comparative structure/expression studies within the genus Haveria. The dicot genus Haveria includes C,-C, intermediate species, as well as C, and C, species. We show that the previously noted differences in NADP-MDH activity levels among C,, C , , and C,-C, Haveria species are in part due to interspecific differences in mRNA accumulation. We also show that the NADP-MDH gene appears to be present as a single copy among different Haveria species, suggesting that a pre-existing gene has been reregulated during the evolution from C, to C, plants to accommodate the abundance and localization requirements of the C, cycle.

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confidence: 88%

Section: Protein Preparation and Analysismentioning

confidence: 99%

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confidence: 94%

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C4 Isoform of NADP-Malate Dehydrogenase (cDNA Cloning and Expression in Leaves of C4, C3, and C3-C4 Intermediate Species of Flaveria)

McGonigle

Nelson

1995

Plant Physiol.

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“…The transcription factor Golden2, which controls chloroplast development in maize PBS cells (Langdale and Kidner, 1994;Hall et al, 1998), resides on maize chromosome 3; however, the absence of changes to chloroplast morphology in either M or PBS cells in OMA 3.01 suggests that it is not active in oat. The argentia mutant impacts on the speed with which patterns of the C 4 mRNAs develop (Langdale et al, 1987), so our analysis of mature OMA leaves is unlikely to have detected phenotypes relevant to determining whether the wild-type ARGENTIA gene product on maize chromosome 9 is active in oat.…”

Section: The Plasticity Of Oat Leaf Anatomymentioning

confidence: 99%

Individual Maize Chromosomes in the C3 Plant Oat Can Increase Bundle Sheath Cell Size and Vein Density

et al. 2012

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C4 photosynthesis has evolved in at least 66 lineages within the angiosperms and involves alterations to the biochemistry, cell biology, and development of leaves. The characteristic “Kranz” anatomy of most C4 leaves was discovered in the 1890s, but the genetic basis of these traits remains poorly defined. Oat × maize addition lines allow the effects of individual maize (Zea mays; C4) chromosomes to be investigated in an oat (Avena sativa; C3) genetic background. Here, we have determined the extent to which maize chromosomes can introduce C4 characteristics into oat and have associated any C4-like changes with specific maize chromosomes. While there is no indication of a simultaneous change to C4 biochemistry, leaf anatomy, and ultrastructure in any of the oat × maize addition lines, the C3 oat leaf can be modified at multiple levels. Maize genes encoding phosphoenolpyruvate carboxylase, pyruvate, orthophosphate dikinase, and the 2′-oxoglutarate/malate transporter are expressed in oat and generate transcripts of the correct size. Three maize chromosomes independently cause increases in vein density, and maize chromosome 3 results in larger bundle sheath cells with increased cell wall lipid deposition in oat leaves. These data provide proof of principle that aspects of C4 biology could be integrated into leaves of C3 crops.

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“…The procedure followed that ofLangdale et al (8) with the addition of an initial gel filtration of the (NH4)2SO4 fraction using a 2.7 x 75 cm Toyopearl HW-55F column followed by DEAE cellulose chromatography (2.4 x 40 cm column). The homogenization solution at pH 7.7 contained 40 mm Tris-HCl, 10 mM MgCl2, 1 mm EDTA, 10 mm 2-mercaptoethanol, and 10% (v/v) glycerol.…”

Section: Enzyme Purificationmentioning

confidence: 99%

Effect of pH on the Kinetic Parameters of NADP-Malic Enzyme from a C₄Flaveria (Asteraceae) Species

Holaday

Lowder²

1989

Plant Physiol.

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We have used the pH variation in the kinetic parameters with respect to malate of NADP-malic enzyme purified from the C4 species, Flaveria trinervia, to compare the pK values of its functional groups with those for the pigeon liver NADP-malic enzyme (Ml Schimerlik, WW Cleland [1977] Biochemistry 16: 576-583) and the plant NAD-malic enzyme (KO Willeford, RT Wedding ] Plant Physiol 84: 1084-1087. Like the other enzymes, the C4 enzyme has a group with a pK of about 6.0 (6.6 for the C4 enzyme), as indicated from plots of the log V,mx/Km (Vmax = maximum rate of catalysis) versus pH, which must lose a proton for malate binding and subsequent catalysis. The optimum ionization for the C4 enzyme-NADP-Mg2+ complex occurs at pH 7.1 to 7.5. From pH 7.5 to 8.4, the Km increases, but V,,., remains constant. The log VmaxIKm plot in this pH range indicates a group with a pK of about 7.7. The other malic enzymes exhibit a similar pK. Above pH 8.4, deprotonation leads to a marked increase in Km and a decrease in V,,, for the C4 enzyme. As in the case of the animal enzyme, the log Vm,x/Km plot for the C4 enzyme appears to approach a slope of two. The curve suggests an average pK of 8.4 for the groups involved, while the animal enzyme exhibits an average pK of 9.0. The NAD-malic enzyme does not exhibit any pK values at these high pK values. We hypothesize that the putative groups with the high pK values may be at least partially responsible for the ability of the C4 NADP-malic enzyme to maintain high activity at pH 8.0 in illuminated chloroplasts.Vma. up to pH 8.0 (7, 10), while the C3 plant enzyme appears to have an optimum activity around pH 6.4 to 7.3 (4, 14). The plant NAD-ME, located in mitochondria, is similar to the C3 NADP-ME with respect to the pH at which it exhibits maximum activity (15). Of course, several factors determine the optimum pH to use for in vitro assays, but a superficial look at all MEs suggests that the C4 enzyme is a special form that has evolved for decarboxylation at high rates in illuminated choroplasts during C4 photosynthesis.Extensive mechanistic information is available for the pigeon liver NADP-ME (7, 10) and is becoming available for plant NAD-ME (15), but such information for the forms of plant NADP-ME is minimal. In light of the differences in the pH optima for the various MEs, we have used the effect of pH on the kinetic parameters with respect to malate for the F. trinervia enzyme as a means of comparing the pK values of functional groups of this putative special form of ME with those published for the pigeon liver enzyme and the plant NAD-ME. MATERIALS AND METHODS Plant MaterialPlants of Flaveria trinervia (Spreng.) C. Mohr were grown in a greenhouse under a 14 h photoperiod during the summer months. The seed was collected locally, and the plants were fertilized with a Hoagland solution three times a week.

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The argentia mutation delays normal development of photosynthetic cell-types in Zea mays

Cited by 74 publications

References 25 publications

C4 Isoform of NADP-Malate Dehydrogenase (cDNA Cloning and Expression in Leaves of C4, C3, and C3-C4 Intermediate Species of Flaveria)

C4 Isoform of NADP-Malate Dehydrogenase (cDNA Cloning and Expression in Leaves of C4, C3, and C3-C4 Intermediate Species of Flaveria)

Individual Maize Chromosomes in the C3 Plant Oat Can Increase Bundle Sheath Cell Size and Vein Density

Effect of pH on the Kinetic Parameters of NADP-Malic Enzyme from a C₄Flaveria (Asteraceae) Species

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The argentia mutation delays normal development of photosynthetic cell-types in Zea mays

Cited by 74 publications

References 25 publications

C4 Isoform of NADP-Malate Dehydrogenase (cDNA Cloning and Expression in Leaves of C4, C3, and C3-C4 Intermediate Species of Flaveria)

C4 Isoform of NADP-Malate Dehydrogenase (cDNA Cloning and Expression in Leaves of C4, C3, and C3-C4 Intermediate Species of Flaveria)

Individual Maize Chromosomes in the C3 Plant Oat Can Increase Bundle Sheath Cell Size and Vein Density

Effect of pH on the Kinetic Parameters of NADP-Malic Enzyme from a C4Flaveria (Asteraceae) Species

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Effect of pH on the Kinetic Parameters of NADP-Malic Enzyme from a C₄Flaveria (Asteraceae) Species