Purification, microsequencing and cloning of spinach ATP‐dependent phosphofructokinase link sequence and function for the plant enzyme

Winkler, Christian; Delvos, Britta; Martin, William; Henze, Katrin

doi:10.1111/j.1742-4658.2006.05590.x

Cited by 27 publications

(30 citation statements)

References 55 publications

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“…ATP is produced by the glycolytic pathway through two reactions catalyzed by 3PGA kinase and pyruvate kinase while UDP-glucose pyrophosphorylase forms UTP that subsequently can be converted into ATP by nucleoside diphosphate kinase. On the other hand, hexokinase and ATP-dependent phosphofructokinase (PFK; Winkler et al, 2007) consume ATP and therefore reduce the net ATP yield of the glycolytic pathway. Moreover, the yield of glycolytic ATP production is affected by several parallel reactions in which ATP is not involved.…”

Section: Regulation Of Glycolytic Activitymentioning

confidence: 99%

Regulation of respiration in plants: A role for alternative metabolic pathways

Dongen

Gupta

Ramírez-Aguilar

et al. 2011

Journal of Plant Physiology

167

127

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Section: Regulation Of Glycolytic Activitymentioning

confidence: 99%

Regulation of respiration in plants: A role for alternative metabolic pathways

Dongen

Gupta

Ramírez-Aguilar

et al. 2011

Journal of Plant Physiology

167

127

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“…In Trichomonas, glycolysis proceeds via a pyrophosphate (PP i )-dependent phosphofructokinase (PP i -PFK) (10), an enzyme that is generally rare in eukaryotes, albeit typical in plants (11). Therefore, it was surprising that genes for ATP-dependent phosphofructokinase (ATP-PFK) turned up in the Trichomonas genome (12).…”

mentioning

confidence: 99%

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis

et al. 2015

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bMitochondrial evolution entailed the origin of protein import machinery that allows nuclear-encoded proteins to be targeted to the organelle, as well as the origin of cleavable N-terminal targeting sequences (NTS) that allow efficient sorting and import of matrix proteins. In hydrogenosomes and mitosomes, reduced forms of mitochondria with reduced proteomes, NTS-independent targeting of matrix proteins is known. Here, we studied the cellular localization of two glycolytic enzymes in the anaerobic pathogen Trichomonas vaginalis: PP i -dependent phosphofructokinase (TvPP i -PFK), which is the main glycolytic PFK activity of the protist, and ATP-dependent PFK (TvATP-PFK), the function of which is less clear. TvPP i -PFK was detected predominantly in the cytosol, as expected, while all four TvATP-PFK paralogues were imported into T. vaginalis hydrogenosomes, although none of them possesses an NTS. The heterologous expression of TvATP-PFK in Saccharomyces cerevisiae revealed an intrinsic capability of the protein to be recognized and imported into yeast mitochondria, whereas yeast ATP-PFK resides in the cytosol. TvATP-PFK consists of only a catalytic domain, similarly to "short" bacterial enzymes, while ScATP-PFK includes an N-terminal extension, a catalytic domain, and a C-terminal regulatory domain. Expression of the catalytic domain of ScATP-PFK and short Escherichia coli ATP-PFK in T. vaginalis resulted in their partial delivery to hydrogenosomes. These results indicate that TvATP-PFK and the homologous ATP-PFKs possess internal structural targeting information that is recognized by the hydrogenosomal import machinery. From an evolutionary perspective, the predisposition of ancient ATP-PFK to be recognized and imported into hydrogenosomes might be a relict from the early phases of organelle evolution.T he transition of the mitochondrion into an ATP-producing organelle was the crucial event at the eukaryote origin (1). ATP synthesis in eukaryotes is typically compartmentalized, with glycolysis in the cytosol and pyruvate oxidation in the mitochondria, which is linked to highly efficient oxidative phosphorylation (1, 2). In protists, however, there are notable exceptions to the usual scheme regarding both glycolysis and pyruvate oxidation. In Trichomonas vaginalis and other eukaryotes that possess an anaerobic form of mitochonria called hydrogenosomes, pyruvate is oxidized within the organelle via less efficient anaerobic fermentation (3). Giardia intestinalis, Entamoeba histolytica, and other eukaryotes possess a reduced form of mitochondria called mitosomes that do not produce ATP at all (4). In these organisms, pyruvate oxidation takes place exclusively in the cytosol (1). In kinetoplastids, glycolysis is compartmentalized in specialized microbodies called glycosomes (5). In some green algae, the first half of the glycolytic pathway is localized in the chloroplast (6, 7), while in the diatom Phaeodactylum tricornutum and other stramenopiles, several glycolytic enzymes are targeted to multiple compartments, such...

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“…In plants, glycolysis is regulated at the transcriptional and allosteric levels and in a complex way due to metabolic flexibility [33,34,64]. In situations when ATP cannot be easily produced in heterotrophic systems (e.g., during hypoxia, chilling, or phosphate starvation), pyrophosphate- instead of ATP-utilizing enzyme forms are used to drive glycolysis [33,34,65,66]. One of the genes encoding phosphofructokinase was up-regulated up to 5.2-fold during winter hardening.…”

Section: Discussionmentioning

confidence: 99%

Evidence for extensive heterotrophic metabolism, antioxidant action, and associated regulatory events during winter hardening in Sitka spruce

Collakova

Klumas²,

Suren

et al. 2013

BMC Plant Biol

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BackgroundCold acclimation in woody perennials is a metabolically intensive process, but coincides with environmental conditions that are not conducive to the generation of energy through photosynthesis. While the negative effects of low temperatures on the photosynthetic apparatus during winter have been well studied, less is known about how this is reflected at the level of gene and metabolite expression, nor how the plant generates primary metabolites needed for adaptive processes during autumn.ResultsThe MapMan tool revealed enrichment of the expression of genes related to mitochondrial function, antioxidant and associated regulatory activity, while changes in metabolite levels over the time course were consistent with the gene expression patterns observed. Genes related to thylakoid function were down-regulated as expected, with the exception of plastid targeted specific antioxidant gene products such as thylakoid-bound ascorbate peroxidase, components of the reactive oxygen species scavenging cycle, and the plastid terminal oxidase. In contrast, the conventional and alternative mitochondrial electron transport chains, the tricarboxylic acid cycle, and redox-associated proteins providing reactive oxygen species scavenging generated by electron transport chains functioning at low temperatures were all active.ConclusionsA regulatory mechanism linking thylakoid-bound ascorbate peroxidase action with “chloroplast dormancy” is proposed. Most importantly, the energy and substrates required for the substantial metabolic remodeling that is a hallmark of freezing acclimation could be provided by heterotrophic metabolism.

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Purification, microsequencing and cloning of spinach ATP‐dependent phosphofructokinase link sequence and function for the plant enzyme

Cited by 27 publications

References 55 publications

Regulation of respiration in plants: A role for alternative metabolic pathways

Regulation of respiration in plants: A role for alternative metabolic pathways

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis

Evidence for extensive heterotrophic metabolism, antioxidant action, and associated regulatory events during winter hardening in Sitka spruce

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