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Open AccessArticle

Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(6), 2039;
Received: 20 February 2020 / Revised: 10 March 2020 / Accepted: 12 March 2020 / Published: 16 March 2020
(This article belongs to the Section Biochemistry)
The effect of protein chaperones HspB6 and the monomeric form of the protein 14-3-3ζ (14-3-3ζm) on a test system based on thermal aggregation of UV-irradiated glycogen phosphorylase b (UV-Phb) at 37 °C and a constant ionic strength (0.15 M) was studied using dynamic light scattering. A significant increase in the anti-aggregation activity of HspB6 and 14-3-3ζm was demonstrated in the presence of 0.1 M arginine (Arg). To compare the effects of these chaperones on UV-Phb aggregation, the values of initial stoichiometry of the chaperone–target protein complex (S0) were used. The analysis of the S0 values shows that in the presence of Arg fewer chaperone subunits are needed to completely prevent aggregation of the UV-Phb subunit. The changes in the structures of HspB6 and 14-3-3ζm induced by binding of Arg were evaluated by the fluorescence spectroscopy and differential scanning calorimetry. It was suggested that Arg caused conformational changes in chaperone molecules, which led to a decrease in the thermal stability of protein chaperones and their destabilization. View Full-Text
Keywords: HspB6; monomeric 14-3-3ζ; anti-aggregation activity; arginine HspB6; monomeric 14-3-3ζ; anti-aggregation activity; arginine
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Mikhaylova, V.V.; Eronina, T.B.; Chebotareva, N.A.; Shubin, V.V.; Kalacheva, D.I.; Kurganov, B.I. Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ. Int. J. Mol. Sci. 2020, 21, 2039.

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