Abstract
Self-association of phosphorylase kinase (PhK) has been studied using analytical ultracentrifugation and dynamic light scattering under the conditions of molecular crowding arising from the presence of high concentrations of osmolyte. Sedimentation velocity analysis shows that in accordance with the predictions of molecular crowding theory, trimethylamine N-oxide (TMAO) greatly favours self-association of PhK induced by α and α . On the contrary, proline suppresses this process, probably, due to its specific interaction with PhK. We have also established that α-crystallin, a protein possessing chaperone-like activity, counteracts the self-association of PhK under molecular crowding conditions. Using dynamic light scattering we have shown that the increase in the light scattering intensity accompanying self-association of PhK is due to the formation of particles having hydrodynamic radius of hundreds of nanometers. The hydrodynamic radius of the start associates (seeds of association) was found to be approximately 80 nm. TMAO facilitates the formation of the associates of larger size whereas proline and α-crystallin suppress self-association of PhK.
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Acknowledgments
This study was funded by the Russian Foundation for Basic Research (grant 05-04-48691), Programs “Molecular and Cell Biology” of the Presidium of the Russian Academy of Sciences, the Program for the Support of the Leading Scientific Schools in Russia (grant 813.2003.4), and by INTAS (grant 03-51-4813).
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Chebotareva, N.A., Meremyanin, A.V., Makeeva, V.F., Kurganov, B.I. Self-Association of Phosphorylase Kinase under Molecular Crowding Conditions. In: Wandrey, C., Cölfen, H. (eds) Analytical Ultracentrifugation VIII. Progress in Colloid and Polymer Science, vol 131. Springer, Berlin, Heidelberg. https://doi.org/10.1007/2882_007
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DOI: https://doi.org/10.1007/2882_007
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