Interaction of phosphofructokinase with tubulin and microtubules: Quantitative evaluation of the mutual effects

A. Lehotzky, Marianna Telegdi, K. Liliom, J. Ovádi

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Abstract

The linked equilibria involved in the binding of phosphofructokinase (EC 2.7.1.11, ATP:D-fructose-6-phosphate 1-phosphotransferase) to tubulin and microtubules were studied at high ionic strength in vitro. The concentration-dependent dissociation of phosphofructokinase was analyzed in the absence and presence of tubulin or microtubules, and the binding of kinase to the tubulin dimer and microtubules was compared. Enzyme activity of phosphofructokinase was inhibited by both tubulin and microtubules: the relative inhibition increased with decreasing enzyme concentration. The complex formation between phosphofructokinase and tubulin was demonstrated by means of fluorescent anisotropy. Concentration-dependent copelleting of the kinase with taxol-stabilized microtubules revealed binding of the enzyme to microtubules as well as phosphofructokinase-enhanced pelleting of microtubules. The binding data agree with the enzyme kinetic findings that the inactive dissociated forms of phosphofructokinase (monomer-dimer) are involved in the heterologous complex formation. Microtubule reorganization (bundle formation) by phosphofructokinase was established by turbidity measurements and sedimentation experiments. The binding data are consistent with a simple molecular model for the interactions in phosphofructokinase-tubulin/microtubules systems.

Original languageEnglish
Pages (from-to)10888-10894
Number of pages7
JournalJournal of Biological Chemistry
Volume268
Issue number15
Publication statusPublished - máj. 25 1993

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Phosphofructokinases
Tubulin
Microtubules
Dimers
Enzymes
Phosphotransferases
Phosphofructokinase-1
Pelletizing
Enzyme kinetics
Enzyme activity
Molecular Models
Turbidity
Paclitaxel
Ionic strength
Anisotropy
Sedimentation
Osmolar Concentration
Monomers

ASJC Scopus subject areas

  • Biochemistry

Cite this

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abstract = "The linked equilibria involved in the binding of phosphofructokinase (EC 2.7.1.11, ATP:D-fructose-6-phosphate 1-phosphotransferase) to tubulin and microtubules were studied at high ionic strength in vitro. The concentration-dependent dissociation of phosphofructokinase was analyzed in the absence and presence of tubulin or microtubules, and the binding of kinase to the tubulin dimer and microtubules was compared. Enzyme activity of phosphofructokinase was inhibited by both tubulin and microtubules: the relative inhibition increased with decreasing enzyme concentration. The complex formation between phosphofructokinase and tubulin was demonstrated by means of fluorescent anisotropy. Concentration-dependent copelleting of the kinase with taxol-stabilized microtubules revealed binding of the enzyme to microtubules as well as phosphofructokinase-enhanced pelleting of microtubules. The binding data agree with the enzyme kinetic findings that the inactive dissociated forms of phosphofructokinase (monomer-dimer) are involved in the heterologous complex formation. Microtubule reorganization (bundle formation) by phosphofructokinase was established by turbidity measurements and sedimentation experiments. The binding data are consistent with a simple molecular model for the interactions in phosphofructokinase-tubulin/microtubules systems.",
author = "A. Lehotzky and Marianna Telegdi and K. Liliom and J. Ov{\'a}di",
year = "1993",
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pages = "10888--10894",
journal = "Journal of Biological Chemistry",
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T1 - Interaction of phosphofructokinase with tubulin and microtubules

T2 - Quantitative evaluation of the mutual effects

AU - Lehotzky, A.

AU - Telegdi, Marianna

AU - Liliom, K.

AU - Ovádi, J.

PY - 1993/5/25

Y1 - 1993/5/25

N2 - The linked equilibria involved in the binding of phosphofructokinase (EC 2.7.1.11, ATP:D-fructose-6-phosphate 1-phosphotransferase) to tubulin and microtubules were studied at high ionic strength in vitro. The concentration-dependent dissociation of phosphofructokinase was analyzed in the absence and presence of tubulin or microtubules, and the binding of kinase to the tubulin dimer and microtubules was compared. Enzyme activity of phosphofructokinase was inhibited by both tubulin and microtubules: the relative inhibition increased with decreasing enzyme concentration. The complex formation between phosphofructokinase and tubulin was demonstrated by means of fluorescent anisotropy. Concentration-dependent copelleting of the kinase with taxol-stabilized microtubules revealed binding of the enzyme to microtubules as well as phosphofructokinase-enhanced pelleting of microtubules. The binding data agree with the enzyme kinetic findings that the inactive dissociated forms of phosphofructokinase (monomer-dimer) are involved in the heterologous complex formation. Microtubule reorganization (bundle formation) by phosphofructokinase was established by turbidity measurements and sedimentation experiments. The binding data are consistent with a simple molecular model for the interactions in phosphofructokinase-tubulin/microtubules systems.

AB - The linked equilibria involved in the binding of phosphofructokinase (EC 2.7.1.11, ATP:D-fructose-6-phosphate 1-phosphotransferase) to tubulin and microtubules were studied at high ionic strength in vitro. The concentration-dependent dissociation of phosphofructokinase was analyzed in the absence and presence of tubulin or microtubules, and the binding of kinase to the tubulin dimer and microtubules was compared. Enzyme activity of phosphofructokinase was inhibited by both tubulin and microtubules: the relative inhibition increased with decreasing enzyme concentration. The complex formation between phosphofructokinase and tubulin was demonstrated by means of fluorescent anisotropy. Concentration-dependent copelleting of the kinase with taxol-stabilized microtubules revealed binding of the enzyme to microtubules as well as phosphofructokinase-enhanced pelleting of microtubules. The binding data agree with the enzyme kinetic findings that the inactive dissociated forms of phosphofructokinase (monomer-dimer) are involved in the heterologous complex formation. Microtubule reorganization (bundle formation) by phosphofructokinase was established by turbidity measurements and sedimentation experiments. The binding data are consistent with a simple molecular model for the interactions in phosphofructokinase-tubulin/microtubules systems.

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