Ethanolic fermentation in transgenic tobacco expressing Zymomonas mobilis pyruvate decarboxylase.

Bucher, Marcel; Brändle, Roland; Kuhlemeier, Cris

doi:10.1002/j.1460-2075.1994.tb06569.x

Cited by 72 publications

(81 citation statements)

References 46 publications

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“…This is much higher than the K m for O 2 of cytochrome oxidase, which is in the low micromolar range. Therefore, the switch from respiration to fermentation is likely to be regulated by an oxygen sensor rather than directly by the terminal oxidase (Bucher et al, 1994). Such a sensor may serve to prioritize the different needs of the cell or tissue (Geigenberger, 2003).…”

Section: The Role Of Oxygen In Pollen Metabolismmentioning

confidence: 99%

“…Cloning of the Zymomonas mobilis PDC gene in the pMON505 expression vector under the control of the 35S promoter of Cauliflower mosaic virus has been described previously (Bucher et al, 1994). The construct was transferred via Agrobacterium tumefaciens LBA 4404 to P. hybrida pdc2/ pdc2 plants (obtained after three backcrosses of the W138 pdc2 allele containing the footprint in the W115 background) using the standard leaf disc transformation method.…”

Section: Plant Transformationmentioning

confidence: 99%

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Pyruvate Decarboxylase Provides Growing Pollen Tubes with a Competitive Advantage in Petunia

et al. 2005

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Rapid pollen tube growth places unique demands on energy production and biosynthetic capacity. The aim of this work is to understand how primary metabolism meets the demands of such rapid growth. Aerobically grown pollen produce ethanol in large quantities. The ethanolic fermentation pathway consists of two committed enzymes: pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH). Because adh mutations do not affect male gametophyte function, the obvious question is why pollen synthesize an abundant enzyme if they could do just as well without. Using transposon tagging in Petunia hybrida, we isolated a null mutant in pollen-specific Pdc2. Growth of the mutant pollen tubes through the style is reduced, and the mutant allele shows reduced transmission through the male, when in competition with wild-type pollen. We propose that not ADH but rather PDC is the critical enzyme in a novel, pollen-specific pathway. This pathway serves to bypass pyruvate dehydrogenase enzymes and thereby maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction.

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Section: The Role Of Oxygen In Pollen Metabolismmentioning

confidence: 99%

Section: Plant Transformationmentioning

confidence: 99%

Pyruvate Decarboxylase Provides Growing Pollen Tubes with a Competitive Advantage in Petunia

et al. 2005

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“…However ethanolic fermentation can also occur under aerobic conditions. For example, it has been shown that PDC and ADH are expressed (and ethanol accumulates) during tobacco pollen development (Bucher et al, 1994(Bucher et al, , 1995Tadege and Kuhlemeier, 1997).…”

Section: How Does the And'andencoded Aldh Mediate Fer-mlity Restoration?mentioning

confidence: 99%

The Genetics, Pathology, and Molecular Biology of T-Cytoplasm Male Sterility in Maize

Wise

Bronson

Schnable

et al. 1999

Advances in Agronomy

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This chapter reviews the genetics, pathology, and molecular biology of T-cytoplasm male sterility in maize. The chapter discusses the role of cytoplasmic male sterility systems in facilitating the production of hybrid seeds. The effects of widespread planting of T-cytoplasm maize on the severe 1970 epidemic and effect of a mitochondria1 gene on disease susceptibility and male sterility are discussed. It also discusses the involvement of nuclear cytoplasmic interactions in restoration of cms-T, the perspectives of cms-T researchers, and future directions. In cms-T plants, male sterility is associated with premature breakdown of the mitochondria-rich, tapetal cell layer of the anther; this layer is crucial to pollen production because it supplies nutrients to the developing microspores. In many species, cms is associated with the expression of novel open-reading frames in the mitochondrial genome. The studies provided a foundation for further research that resulted in the cloning of the T-urf13 and Rf2 genes from maize and the ChPKSl gene from C. heterostrophus, and the generation of models for the topology of urf13 in the inner mitochondrial membrane, Rfl-mediated processing of T-urfl3 transcripts, and the evolution of toxin biosynthesis in C. heterostrophus and M. zeae-maydis. Disciplines Agronomy and Crop Sciences | Botany | Plant Breeding and Genetics | Plant Pathology CommentsThis is a chapter from Advances in Agronomy 65 (1999): 79,

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“…Though cloned from plants and fungi (25,38), only bacterial PDC enzymes are produced at high levels as active recombinant products (6,10,11,34,40,45). Recombinant Z. mobilis PDC has been used for the metabolic engineering of ethanol pathways in many organisms (4,8,14,16,22,44). …”

mentioning

confidence: 99%

Cloning and Characterization of the Zymobacter palmae Pyruvate Decarboxylase Gene ( pdc ) and Comparison to Bacterial Homologues

Krishnan

Talarico

Ingram

et al. 2002

Appl Environ Microbiol

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Pyruvate decarboxylase (PDC) is the key enzyme in all homo-ethanol fermentations. Although widely distributed among plants, yeasts, and fungi, PDC is absent in animals and rare in bacteria (established for only three organisms). Genes encoding the three known bacterial pdc genes have been previously described and expressed as active recombinant proteins. The pdc gene from Zymomonas mobilis has been used to engineer ethanol-producing biocatalysts for use in industry. In this paper, we describe a new bacterial pdc gene from Zymobacter palmae. The pattern of codon usage for this gene appears quite similar to that for Escherichia coli genes. In E. coli recombinants, the Z. palmae PDC represented approximately 1/3 of the soluble protein.Biochemical and kinetic properties of the Z. palmae enzyme were compared to purified PDCs from three other bacteria. Of the four bacterial PDCs, the Z. palmae enzyme exhibited the highest specific activity (130 U mg of protein ؊1 ) and the lowest K m for pyruvate (0.24 mM). Differences in biochemical properties, thermal stability, and codon usage may offer unique advantages for the development of new biocatalysts for fuel ethanol production.Pyruvate decarboxylase (PDC) is the key enzyme for all homo-fermentative ethanol pathways. This enzyme catalyzes the nonoxidative decarboxylation of pyruvate to acetaldehyde using Mg 2ϩ and thiamine pyrophosphate (TPP) as cofactors. Acetaldehyde is reduced to ethanol by alcohol dehydrogenase (ADH) during NADH oxidation. ADH enzymes are widely distributed throughout nature (41). In contrast, PDC is common to only plants, yeasts, and fungi; it is absent in animals and rare in prokaryotes (25). PDC has been established by cloning and purification for only three bacteria, Zymomonas mobilis (6,7,11,19,33,34), Sarcina ventriculi (28,45), and Acetobacter pasteurianus (40). Though cloned from plants and fungi (25,38), only bacterial PDC enzymes are produced at high levels as active recombinant products (6,10,11,34,40,45). Recombinant Z. mobilis PDC has been used for the metabolic engineering of ethanol pathways in many organisms (4,8,14,16,22,44).An ethanologenic bacterium, Zymobacter palmae, has been reported which appears to contain a PDC enzyme (37). Z. palmae was originally isolated from palm sap (37) and produces ethanol as a primary fermentation product from a variety of hexose sugars and saccharides (20,36). This bacterium is distinct from other ethanol-fermenting bacteria including those belonging to the genera Zymomonas. Zymomonas is well known for production of ethanol from plant sap in tropical areas; however, its fermentable carbohydrates are limited to glucose, fructose, and saccharose (22). In addition to substrate utilization, Zymobacter (55.8 Ϯ 0.4 mol% GϩC) differs dramatically from Zymomonas (48.5 Ϯ 0.5 mol% GϩC) in genome composition. This is consistent with the other phenotypic differences that have been observed, including the type of ubiquinone synthesized and peritrichous versus polar flagellation (37).In this paper, we have establis...

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Ethanolic fermentation in transgenic tobacco expressing Zymomonas mobilis pyruvate decarboxylase.

Cited by 72 publications

References 46 publications

Pyruvate Decarboxylase Provides Growing Pollen Tubes with a Competitive Advantage in Petunia

Pyruvate Decarboxylase Provides Growing Pollen Tubes with a Competitive Advantage in Petunia

The Genetics, Pathology, and Molecular Biology of T-Cytoplasm Male Sterility in Maize

Cloning and Characterization of the Zymobacter palmae Pyruvate Decarboxylase Gene ( pdc ) and Comparison to Bacterial Homologues

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