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  Use of biomolecular interaction analysis to elucidate the regulatory mechanism of the cysteine synthase complex from <i>Arabidopsis thaliana</i>

Berkowitz, O., Wirtz, M., Wolf, A., Kuhlmann, J., & Hell, R. (2002). Use of biomolecular interaction analysis to elucidate the regulatory mechanism of the cysteine synthase complex from <i>Arabidopsis thaliana</i>. Journal of Biological Chemistry, 277(34): 1, pp. 30629-30634. Retrieved from http://www.jbc.org/cgi/reprint/277/34/30629.pdf.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Biol. Chem.

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 Urheber:
Berkowitz, Oliver, Autor
Wirtz, Markus, Autor
Wolf, Alexander1, Autor
Kuhlmann, Jürgen2, Autor           
Hell, Rüdiger, Autor
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753294              

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 Zusammenfassung: Real time biomolecular interaction analysis based on surface plasmon resonance has been proven useful for studying protein- protein interaction but has not been extended so far to investigate enzyme-enzyme interactions, especially as pertaining to regulation of metabolic activity. We have applied BIAcore technology to study the regulation of enzyme-enzyme interaction during mitochondrial cysteine biosynthesis in <i>Arabidopsis thaliana</i>. The association of the two enzyme subunits in the hetero-oligomeric cysteine synthase complex was investigated with respect to the reaction intermediate and putative effector O-acetylserine. We have determined an equilibrium dissociation constant of the cysteine synthase complex (<i>K</i>D = 25 ± 4 x 10-9 M), based on a reliable A + B <=> AB model of interaction. Analysis of dissociation kinetics in the presence of O-acetylserine revealed a half-maximal dissociation rate at 77 ± 4 ?M O-acetylserine and strong positive cooperativity for complex dissociation. The equilibrium of interaction was determined using an enzyme activity-based approach and yielded a <i>K</i>m value of 58 ± 7 ?M O-acetylserine. Both effector concentrations are in the range of intracellular O-acetylserine fluctuations and support a functional model that integrates effector-driven cysteine synthase complex dissociation as a regulatory switch for the biosynthetic pathway. The results show that BIAcore technology can be applied to obtain quantitative kinetic data of a hetero-oligomeric protein complex with enzymatic and regulatory function

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Sprache(n): eng - English
 Datum: 2002-08-23
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 6093
URI: http://www.jbc.org/cgi/reprint/277/34/30629.pdf
 Art des Abschluß: -

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Titel: Journal of Biological Chemistry
  Alternativer Titel : J. Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 277 (34) Artikelnummer: 1 Start- / Endseite: 30629 - 30634 Identifikator: -