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Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

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Abstract

Effects of α-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) have been studied using dynamic light scattering and analytical ultracentrifugation. The analysis of the initial parts of the dependences of the hydrodynamic radius of protein aggregates on time shows that in the presence of α-crystallin or GroEL the kinetic regime of GAPDH aggregation is changed from the regime of diffusion-limited cluster–cluster aggregation to the regime of reaction-limited cluster–cluster aggregation, wherein the sticking probability for the colliding particles becomes lower the unity. In contrast to α-crystallin, GroEL does not interfere with formation of the start aggregates which include denatured GAPDH molecules. On the basis of the analytical ultracentrifugation data the conclusion has been made that the products of dissociation of GAPDH and α-crystallin or GroEL play an important role in the interactions of GAPDH and chaperones at elevated temperatures.

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Abbreviations

DLCA:

Diffusion-limited cluster–cluster aggregation

DLS:

Dynamic light scattering

DSC:

Differential scanning calorimetry

GAPDH:

Glyceraldehyde-3-phosphate dehydrogenase

RLCA:

Reaction-limited cluster–cluster aggregation

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Acknowledgments

This study was funded by the Russian Foundation for Basic Research (grants 08-04-00666-a, 08-04-00231_a and 08-08-00540_a), the Program “Molecular and Cell Biology” of the Presidium of the Russian Academy of Sciences and CNTP (Russia, 02.512.11.2249).

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Authors and Affiliations

  1. Bach Institute of Biochemistry, Russian Academy of Sciences, 119071, Moscow, Russia

    Kira A. Markossian, Nikolay V. Golub, Natalia A. Chebotareva & Boris I. Kurganov

  2. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992, Moscow, Russia

    Regina A. Asryants, Irina N. Naletova & Vladimir I. Muronetz

  3. Faculty of Bioengineering and Bioinformatics, Moscow State University, 119992, Moscow, Russia

    Vladimir I. Muronetz

  4. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia

    Konstantin O. Muranov

Authors
  1. Kira A. Markossian
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Correspondence to Kira A. Markossian.

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Markossian, K.A., Golub, N.V., Chebotareva, N.A. et al. Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase. Protein J 29, 11–25 (2010). https://doi.org/10.1007/s10930-009-9217-9

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