Immobilized d‐glyceraldehyde‐3‐phosphate dehydrogenase can exist as a trimer

Ashmarina, L.I.; Muronetz, Vladimir I.; Nagradova, N.K.

doi:10.1016/0014-5793(81)81069-1

Cited by 20 publications

(15 citation statements)

References 11 publications

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“…At the same time, the possibility of specific association between PGK and GPDH was demonstrated by physico-chemical methods [8][9][10][11]. The results obtained were in line with the suggestion that the strength of the bienzyme association varied depending on the source of the enzymes.…”

Section: Introductionsupporting

confidence: 68%

“…In the variety of physico-chemical methods used thus far to study associations between glycolytic enzymes, the technique based on matrix immobilization, first introduced by Beekmans and Kanarek [18], seems to be among the most appealing. Using this approach, we have demonstrated specific association between rabbit muscle GPDH and lactate dvhydrogenase [19], as well as between GPDH and PGK isolated from baker's yeast [8] and rabbit muscle [9910].…”

Section: Discussionmentioning

confidence: 99%

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Interaction between d‐glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase and its functional consequences

1992

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E. cob D-glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble E. coR 3-phosphoglycerate kinase with a stoichiometry of 1.77~_0.61 kinase molecules per tetramer of the dehydrogenase and an apparent K., of 1.03+0.68/tM (10 mM sodium phosphate, 0.15 M Noel). No interaction was detected between E. colt t>glyceraldehyde-3-phosphate dehydrog~nase and rabbit muscle 3.phosphoglycerate kinase. The species-specificity of the bienzyme association made it possible to develop a kinetic approach to demonstrate the functionally significant interaction between E. colt o-glyceraldehyde-3-phosphate dehydrogenase and E. colt 3.phosphoglycerate kinase, which consists of an increase in steady-state rate of the coupled reaction.~.Clyeeraldehyde.3-phosphate dehydrogenase; 3-Phosphoglycerate kinase; Bienzyme complex

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Section: Introductionsupporting

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Interaction between d‐glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase and its functional consequences

1992

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“…The evidence for GPDH . PGK complex formation was obtained in our studies on yeast enzymes [5] as well as on the enzymes isolated from rabbit muscle [6,7]. Using the technique of enzyme immobilization on a solid support, we could show a specific association between matrix-bound GPDH and soluble PGK under the conditions when the enzymes were functioning.…”

Section: Introductionmentioning

confidence: 51%

Association of rabbit muscle glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase The biochemical and electron‐microscopic evidence

et al. 1988

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Rabbit muscle glyceraldehyde‐3‐phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3‐phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme‐3‐phosphoglycerol·NADH complex. The substrate‐free 3‐phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3‐diphosphoglycerate. Electron‐microscopic evidence for the association of the soluble acyl‐glyceraldehyde‐3‐phosphate dehydrogenase·NADH complex and 3‐phosphoglycerate kinase was also obtained.

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“…Association of GAPD with polyrisobomes could thus be advantageous regarding the energy supply for translation, since it would allow high-energy compounds to be produced at the site of their utilization. The next enzyme in the glycolytic pathway, phosphoglycerate kinase, which produces ATP, can also be associated with polyribosomes since it can form a complex with GAPD [15,16] and can also bind RNA (data not shown). The production of nucleoside triphosphates by the two-enzyme system GAPD/phosphoglycerate kinase has a further advantage for protein synthesis in comparison with other energy-providing systems.…”

Section: Discussionmentioning

confidence: 99%

Association of glyceraldehyde‐3‐phosphate dehydrogenase with mono‐and polyribosomes of rabbit reticulocytes

Ryazanov

Ashmarina

Muronetz

1988

European Journal of Biochemistry

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It has been shown recently that glyceraldehyde-3-phosphate dehydrogenase (GAPD) is one of the three major RNA-binding proteins ofrabbit reticulocytes [Ryazanov, A. G. (1985) FEBS Lett. 192,131 -1341. It was suggested that, due to its RNA-binding capacity, GAPD can form loose dynamic complexes with polyribosomes.This communication reports that a considerable amount of GAPD activity can be found in the mono-and polyribosome fraction after sucrose gradient centrifugation of rabbit reticulocyte lysate. An increase of ionic strength, as well as the addition of exogenous RNA to the extract, result in the removal of GAPD from the complex with mono-and polyribosomes. It appears that GAPD forms the complex with polyribosomes due to the interaction with some exposed RNA regions of these structures. Although the interaction of GAPD with ribosomes is weak, it can be detected under physiological ionic conditions by the difference boundary sedimentation velocity technique.Association of GAPD with mono-and polyribosomes can be prevented by a low concentration (10 pM) of NADH, but not NAD'. A nitrocellulose filter binding assay also shows that NADH has a stronger inhibitory effect on the enzyme-RNA complex formation, as compared with NAD'.We propose that the RNA-mediated association of GAPD with mono-and polyribosomes can provide compartmentation of the energy-supplying system on these structures within the cell. This can maintain a high local concentration of ATP and GTP near the sites of protein synthesis.In the cytoplasm of a eukaryotic cell there is a fraction of proteins with an affinity for high-polymer polynucleotides (RNA-binding proteins). This fraction contains the proteins of the translation machinery, such as elongation and initiation factors and aminoacyl-tRNA synthetases (see reviews [I -31).The nonspecific affinity for RNA is a characteristic feature of the eukaryotic proteins involved in translation, whereas the prokaryotic elongation factors and aminoacyl-tRNA synthetases have no affinity for RNA [l-31. Elongation factors, aminoacyl-tRNA synthetases and some other RNAbinding proteins can form loose complexes with mono-and polyribosomes due to their RNA-binding capacity (see reviews [l -31). This suggests that the nonspecific affinity for RNA can result in compartmentation of proteins of the translational apparatus on polyribosomes in a large and intricately arranged eukaryotic cell [l -41. According to SDS-electrophoresis data, RNA-binding proteins of rabbit reticulocytes contain three major components (molecular mass 96 kDa, 49 kDa and 36 kDa) and many minor ones [5]. The 96-kDa and 49-kDa polypeptides have been identified previously as elongation factors EF-2 and EF-la, respectively [6, 71. The third major component, the 36-kDa polypeptide, has been identified as a glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPD) [81.

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Immobilized d‐glyceraldehyde‐3‐phosphate dehydrogenase can exist as a trimer

Cited by 20 publications

References 11 publications

Interaction between d‐glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase and its functional consequences

Interaction between d‐glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase and its functional consequences

Association of rabbit muscle glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase The biochemical and electron‐microscopic evidence

Association of glyceraldehyde‐3‐phosphate dehydrogenase with mono‐and polyribosomes of rabbit reticulocytes

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