Studies on the structure of yeast phosphofructokinase

Chaffotte, Alain; Laurent, Michel; Tijane, M'hamed; Tardieu, A.; Roucous, Colette; Seydoux, François; Yon, Jeannine

doi:10.1016/0300-9084(84)90191-3

Cited by 11 publications

(6 citation statements)

References 39 publications

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“…This value is nearly 300 × higher than in D. discoideum cells (6.5 × 10-3% [12]). The enzyme was also overexpressed with respect to native yeast PFK, since the later is ~0.5% of extract protein [33,34]. After completion of this work, we observed that the recombi- nant enzyme can also be obtained pure by omitting the polyethylene glycol fractionation step (Table 1), although with a yield of only 7%.…”

Section: Purification and Properties Of The Recombinant Enzymementioning

confidence: 91%

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Functional complementation of yeast phosphofructokinase mutants by the non‐allosteric enzyme from Dictyostelium discoideum

1995

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Phosphofructokinase (PFK) from yeast has been replaced by the non-allosteric isozyme from the slime mold Dictyostelium discoideum. This has been achieved by overexpression of the latter in a PFK-deficient strain of Saccharomyces cerevisiae under the control of the PFK2 promoter. Transformants complemented the glucose-negative growth phenotype exhibiting generation times on glucose-containing media similar to those of an untransformed strain being wild-type for yeast PFK genes. The PFK produced reacted with an antibody against D. discoideum PFK. It exhibited the same subunit size, quaternary structure and kinetic parameters than those of the wild-type enzyme, and was also devoid of specific regulatory properties.

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Section: Purification and Properties Of The Recombinant Enzymementioning

confidence: 91%

“…Spain. Fax: (34) (1) 3975353. tive binding sites for effectors (Est6vez, A.M., Martinez-Costa, O.H., Sfinchez, V. and Arag6n, J.J., in prep.). PFK activity in the slime mold is scarce, ~0.5-1.2 U/g wet mass [12].…”

Section: Introductionmentioning

confidence: 99%

Functional complementation of yeast phosphofructokinase mutants by the non‐allosteric enzyme from Dictyostelium discoideum

1995

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“…Although the techniques described above give generally good results concerning the molecular mass estimations of proteins, it is well known that the results depend very much on the shape and on the charge of the polypeptides and also on the molecular mass markers used [27]. It has also been recently described that amphiphilic proteins, such as membrane peripheral enzymes, exhibit self-association behavior in aqueous media, even in the presence of SDS, since detergents are often insufficient to disrupt all the interactions between the protein molecules or between domains of a single molecule [28].…”

Section: Resultsmentioning

confidence: 99%

Structural, immunological and kinetic comparisons of NADP‐dependent malate dehydrogenases from spinach (C₃) and corn (C₄) chloroplasts

Ferté

Jacquot

Meunier

1986

European Journal of Biochemistry

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This paper compares structural, immunological and kinetic properties of corn (C,) and spinach (C,) NADPmalate dehydrogenases. These chloroplastic enzymes are regulated in vivo by thiol -disulfide interchange. Both in their oxidized (inactive) and reduced (active) states these enzymes have a dimeric structure with molecular masses for the subunit ranging from 28 kDa to 38 kDa according to the procedure used for the determination. These enzymes are thus structurally related. The use of specific antibodies showed that they are also immunologically related although not identical. Finally both enzymes showed close kinetic properties with comparable k,,, and K,. Since C, plants have approximately ten times more NADP-malate dehydrogenase activity than C3 plants, these data suggest that the differences in activities are probably related to the enzyme content of each plant type.N ADH-dependent malate dehydrogenases are ubiquitous enzymes, isoenzymes of which are found in bacteria, mammals and plants [l]. The latter organisms, however, possess a unique NADPH-dependent malate dehydrogenase (NADP-MDH). The most striking difference between the NADH and the NADPH-dependent malate dehydrogenases is that the latter, unlike its NADH counterparts, is regulated by its redox status [2, 31. Indeed, the NADP-malate dehydrogenase is in vivo activated by light and inactivated in the dark [4, 51. Studies of the activation/inactivation mechanism have led to the discovery of a light-dependent modification system, endogeneous to the chloroplast, called the ferredoxin-thioredoxin system, which can be reconstituted in vitro and comprises isolated thylakoids and the following soluble proteins: ferredoxin, ferredoxin-thioredoxin reductase and thioredoxins [6, 71. Photochemically or chemically (dithiothreitol) reduced thioredoxins can, in turn, activate the NADP-malate dehydrogenase presumably via a thiol -disulfide interchange mechanism with the appearance of new thiol groups on the enzyme together with the catalytic activity [8, 91. NADP-MDH can also be reduced by dithiothreitol alone with a lower efficiency through a similar mechanism [lo-121.NADP-malate dehydrogenase is present only in the chloroplasts of C3 and C4 mesophyll plant cells [13,14]. While it seems to be clear that in C4 leaves it is involved in the soCorrespvndence to J

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“…10,11 By contrast, Saccharomyces cerevisiae PFK (ScPFK) forms stable heterooctamers α 4 β 4 with a molecular mass of ∼ 800 kDa and a sedimentation coefficient 21S. 12,13 Both α and β subunits are homologous to each other and show an internal sequence duplication similar to that seen in mammalian PFKs. 14 It has been proposed that gene duplications lead to a functional diversification of the multiplied catalytic and effector sites, allowing eukaryotes to develop their relatively more complex control apparatus for glycolytic processes.…”

Section: Introductionmentioning

confidence: 95%

The Crystal Structures of Eukaryotic Phosphofructokinases from Baker's Yeast and Rabbit Skeletal Muscle

Banaszak

Mechin

Obmolova

et al. 2011

Journal of Molecular Biology

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Studies on the structure of yeast phosphofructokinase

Cited by 11 publications

References 39 publications

Functional complementation of yeast phosphofructokinase mutants by the non‐allosteric enzyme from Dictyostelium discoideum

Functional complementation of yeast phosphofructokinase mutants by the non‐allosteric enzyme from Dictyostelium discoideum

Structural, immunological and kinetic comparisons of NADP‐dependent malate dehydrogenases from spinach (C₃) and corn (C₄) chloroplasts

The Crystal Structures of Eukaryotic Phosphofructokinases from Baker's Yeast and Rabbit Skeletal Muscle

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Studies on the structure of yeast phosphofructokinase

Cited by 11 publications

References 39 publications

Functional complementation of yeast phosphofructokinase mutants by the non‐allosteric enzyme from Dictyostelium discoideum

Functional complementation of yeast phosphofructokinase mutants by the non‐allosteric enzyme from Dictyostelium discoideum

Structural, immunological and kinetic comparisons of NADP‐dependent malate dehydrogenases from spinach (C3) and corn (C4) chloroplasts

The Crystal Structures of Eukaryotic Phosphofructokinases from Baker's Yeast and Rabbit Skeletal Muscle

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Structural, immunological and kinetic comparisons of NADP‐dependent malate dehydrogenases from spinach (C₃) and corn (C₄) chloroplasts