Purification and characterization of pyrophosphate- and ATP-dependent phosphofructokinases from banana fruit

Turner, William L.; Plaxton, William C.

doi:10.1007/s00425-002-0962-7

Cited by 32 publications

(16 citation statements)

References 41 publications

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“…Neither subunit composition nor the size of the protein was similar in all plant species tested. One major problem in PFK isolation was the instability of the enzyme during purification [22,27]. However, as a consistent result, cytosolic and plastidic isoforms were found in many plant species (Table 1), as known for several glycolytic enzymes [1].…”

Section: Introductionmentioning

confidence: 74%

“…While PFP has been studied in detail, plant PFK has received only little attention. Besides extensive studies of Musa cavendishii PFKs [18][19][20][21][22], the enzyme was analysed in Daucus carota, Cucumis sativus, Solanum tuberosum, Ricinus communis, and Spinacia oleracea [23][24][25][26][27][28][29][30][31][32] (see Table 1 for details). Neither subunit composition nor the size of the protein was similar in all plant species tested.…”

Section: Introductionmentioning

confidence: 99%

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Characterisation of the ATP‐dependent phosphofructokinase gene family from Arabidopsis thaliana

2007

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Plants possess two different types of phosphofructokinases, an ATP-dependent (PFK) and a pyrophosphate-dependent form (PFP). While plant PFPs have been investigated in detail, cDNA clones coding for PFK have not been identified in Arabidopsis thaliana. Searching the A. thaliana genome revealed 11 putative members of a phosphofructokinase gene family. Among those, four sequences showed high homology to the alpha-or beta-subunits of plant PFPs. Seven cDNAs resulted in elevated PFK, but not PFP activity after transient expression in tobacco leaves suggesting that they encode Arabidopsis PFKs. RT-PCR revealed different tissue-specific expression of the individual forms. Furthermore, analysis of GFP fusion proteins indicated their presence in different sub-cellular compartments.

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Section: Introductionmentioning

confidence: 74%

Section: Introductionmentioning

confidence: 99%

Characterisation of the ATP‐dependent phosphofructokinase gene family from Arabidopsis thaliana

2007

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“…In 1975, Latzko & Kelly [22] reported the existence of chloroplast-and cytosol-specific isoenzymes in spinach. Since then, the isoforms of ATP-PFK from various plant sources have been studied [23][24][25][26][27][28][29][30][31][32][33][34]. Spinach cytosolic ATP-PFK is activated by 25 mm phosphate, whereas the chloroplast enzyme is slightly inhibited [27,28,[30][31][32].…”

Section: Databasementioning

confidence: 99%

“…ATP-PFK from potato tubers was purified to apparent homogeneity; the final prepartion was reported to consist of four different subunits (PFK a-d ) with molecular masses of 46 300, 49 500, 50 000 and 53 000 kDa, respectively [33]. More recently, two isoforms of ATP-PFK from banana fruit with native molecular masses of 210 and 160 kDa, respectively, but of unknown subunit composition, were partially purified [34]. However, plant ATP-PFK activity has never been experimentally linked to any specific protein sequence, because no purified ATP-PFK from any plant source has been sequenced to date, and nor has ATP-PFK activity been demonstrated for any putative plant ATP-PFK gene product by recombinant expression in heterologous systems.…”

Section: Databasementioning

confidence: 99%

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

Winkler¹,

Delvos²,

Martin³

et al. 2006

The FEBS Journal

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Despite its importance in plant metabolism, no sequences of higher plant ATP‐dependent phosphofructokinase (EC 2.7.1.11) are annotated in the databases. We have purified the enzyme from spinach leaves 309‐fold to electrophoretic homogeneity. The purified enzyme was a homotetramer of ∼52 kDa subunits with a specific activity of 600 mU·mg−1 and a Km value for ATP of 81 µm. The purified enzyme was not activated by phosphate, but slightly inhibited instead, suggesting that it was the chloroplast isoform. The inclusion of adenosine 5′‐(β,γ‐imido)triphosphate was conducive to enzyme activitiy during the purification protocol. The sequences of eight tryptic peptides from the final protein preparation, which did not utilize pyrophosphate as a phosphoryl donor, were determined and an exactly corresponding cDNA was cloned. The sequence of enzymatically active spinach ATP‐dependent phosphofructokinase suggests that a large family of genomics‐derived higher plant sequences currently annotated in the databases as putative pyrophosphate‐dependent phosphofructokinases according to sequence similarity is misannotated with respect to the cosubstrate.

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“…Indeed, PFK isoforms of various plant species were found in chloroplasts and in the cytosol (Cawood et al, 1988; Knowles et al, 1990; Turner and Plaxton, 2003). While cytosolic PFKs catalyze a step in the normal cytosolic glycolysis for energy metabolism, plastidal glycolysis using plastidal PFK contributes to starch breakdown and generation of metabolites for biosynthetic processes in dark-adapted or non-photosynthetic plastids (Plaxton, 1996).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Phosphofructokinase Gene Family in Rice and Its Expression Under Oxygen Deficiency Stress

et al. 2013

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Plants possess two types of phosphofructokinase proteins for phosphorylation of fructose-6-phosphate, the ATP-dependent phosphofructokinase (PFK) and the pyrophosphate-(PPi) dependent pyrophosphate-fructose-6-phosphate-phosphotransferase (PFP). During oxygen deficiency ATP levels in rice seedlings are severely reduced, and it is hypothesized that PPi is used as an alternative energy source for the phosphorylation of fructose-6-phosphate during glycolysis. In this study, we analyzed the expression of 15 phosphofructokinase-encoding genes in roots and aerial tissues of anoxia-tolerant rice seedlings in response to anoxic stress and compared our data with transcript profiles obtained from microarray analyses. Furthermore, the intracellular localization of rice PFK proteins was determined, and the PFK and PFP isoforms were grouped in a phylogenetic tree. Two PFK and two PFP transcripts accumulated during anoxic stress, whereas mRNA levels of four PFK and three PFP genes were decreased. The total specific activity of both PFK and PFP changed only slightly during a 24-h anoxia treatment. It is assumed that expression of different isoforms and their catalytic properties differ during normoxic and anoxic conditions and contribute to balanced glycolytic activity during the low-oxygen stress. These characterizations of phosphofructokinase genes and the comparison to other plant species allowed us to suggest candidate rice genes for adaptation to anoxic stress.

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Purification and characterization of pyrophosphate- and ATP-dependent phosphofructokinases from banana fruit

Cited by 32 publications

References 41 publications

Characterisation of the ATP‐dependent phosphofructokinase gene family from Arabidopsis thaliana

Characterisation of the ATP‐dependent phosphofructokinase gene family from Arabidopsis thaliana

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

Characterization of the Phosphofructokinase Gene Family in Rice and Its Expression Under Oxygen Deficiency Stress

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