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

• Published in: International journal of molecular sciences Vol. 21; no. 6; p. 2039
• Main Authors: Mikhaylova, Valeriya V, Eronina, Tatiana B, Chebotareva, Natalia A, Shubin, Vladimir V, Kalacheva, Daria I, Kurganov, Boris I
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 16-03-2020; MDPI
• Subjects: 14-3-3 Proteins - chemistry; Aggregates; anti-aggregation activity; Apoptosis; Arginine; Arginine - chemistry; Calorimetry, Differential Scanning; Cell adhesion & migration; Cell division; Chaperones; Destabilization; Differential scanning calorimetry; Dynamic Light Scattering; Fluorescence; Fluorescence spectroscopy; Glycogen; Glycogen phosphorylase; Glycogens; HSP20 Heat-Shock Proteins - chemistry; hspb6; Humans; Ionic strength; Kinetics; Light; Light scattering; Macromolecular Substances - chemistry; Molecular Chaperones - chemistry; monomeric 14-3-3ζ; Osmolar Concentration; Phosphorylase; Phosphorylases; Photon correlation spectroscopy; Physiology; Protein Aggregates; Protein Conformation; Protein Folding; Proteins; Stoichiometry; Test systems; Thermal stability; anti-aggregation activity; arginine; HspB6; monomeric 14-3-3ζ
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms21062039

The effect of protein chaperones HspB6 and the monomeric form of the protein 14-3-3ζ (14-3-3ζ
) on a test system based on thermal aggregation of UV-irradiated glycogen phosphorylase
(UV-Ph
) 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 14-3-3ζ
was demonstrated in the presence of 0.1 M arginine (Arg). To compare the effects of these chaperones on UV-Ph
aggregation, the values of initial stoichiometry of the chaperone-target protein complex (
) were used. The analysis of the
values shows that in the presence of Arg fewer chaperone subunits are needed to completely prevent aggregation of the UV-Ph
subunit. The changes in the structures of HspB6 and 14-3-3ζ
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.