Dual effect of arginine on aggregation of phosphorylase kinase

Eronina, Tatiana B.; Chebotareva, Natalia A.; Sluchanko, Nikolai N.; Mikhaylova, Valeriya V.; Makeeva, Valentina F.; Roman, Svetlana G.; Kleymenov, Sergey Y.; Bi, Kurganov

doi:10.1016/j.ijbiomac.2014.04.056

Cited by 17 publications

(3 citation statements)

References 65 publications

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“…It was suggested that in this case the formation of larger aggregates and, as a result, acceleration of UV-Phb aggregation is due to conformational destabilization of UV-Phb molecules in the presence of Arg, which is due to the interaction of the guanidine group of arginine and acidic residues of the protein. Similar data were obtained for aggregation of bovine serum albumin (BSA) at 70 • C [45], for dithiothreitol-induced aggregation of BSA at 45 • C [46] and for aggregation of phosphorylase kinase from rabbit skeletal muscle in the presence of 0.1 mM EGTA at 37 • C [34]. When UV-Phb interacts with HspB6 or 14-3-3ζ m , the value of R h * also increases ( Table 1).…”

Section: Discussionsupporting

confidence: 74%

“…The role of Arg in specific and non-specific protein-protein interactions was reviewed in the works [30][31][32][33]. However, it should be noted that Arg can not only suppress, but also enhance the aggregation of the target protein [34][35][36]. In addition, Arg has been shown to regulate the anti-aggregation activity of some sHsps (α-crystallin, HspB5 and HspB4) [37][38][39].…”

Section: Introductionmentioning

confidence: 99%

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

Mikhaylova

Eronina

Chebotareva

et al. 2020

IJMS

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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.

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Section: Discussionsupporting

confidence: 74%

Section: Introductionmentioning

confidence: 99%

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

Mikhaylova

Eronina

Chebotareva

et al. 2020

IJMS

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“…However, sometimes as in case of aggregation of bovine catalase at 55 °C, 0.1 M Arg reduces activity of αB-Cr [ 29 ]. Moreover, sometimes Arg acts on PPIs in two opposite ways depending on the environmental conditions [ 31 ]. Thus, the effect of Arg on the chaperone activity of αB-Cr is the target protein-specific.…”

Section: Introductionmentioning

confidence: 99%

Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b

Eronina

Mikhaylova

Chebotareva

et al. 2022

IJMS

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Protein–protein interactions (PPIs) play an important role in many biological processes in a living cell. Among them chaperone–client interactions are the most important. In this work PPIs of αB-crystallin and glycogen phosphorylase b (Phb) in the presence of betaine (Bet) and arginine (Arg) at 48 °C and ionic strength of 0.15 M were studied using methods of dynamic light scattering, differential scanning calorimetry, and analytical ultracentrifugation. It was shown that Bet enhanced, while Arg reduced both the stability of αB-crystallin and its adsorption capacity (AC0) to the target protein at the stage of aggregate growth. Thus, the anti-aggregation activity of αB-crystallin increased in the presence of Bet and decreased under the influence of Arg, which resulted in inhibition or acceleration of Phb aggregation, respectively. Our data show that chemical chaperones can influence the tertiary and quaternary structure of both the target protein and the protein chaperone. The presence of the substrate protein also affects the quaternary structure of αB-crystallin, causing its disassembly. This is inextricably linked to the anti-aggregation activity of αB-crystallin, which in turn affects its PPI with the target protein. Thus, our studies contribute to understanding the mechanism of interaction between chaperones and proteins.

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