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

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 °...

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Autores principales: Eronina, Tatiana B., Mikhaylova, Valeriya V., Chebotareva, Natalia A., Tugaeva, Kristina V., Kurganov, Boris I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8998655/
https://www.ncbi.nlm.nih.gov/pubmed/35409175
http://dx.doi.org/10.3390/ijms23073816
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author Eronina, Tatiana B.
Mikhaylova, Valeriya V.
Chebotareva, Natalia A.
Tugaeva, Kristina V.
Kurganov, Boris I.
author_facet Eronina, Tatiana B.
Mikhaylova, Valeriya V.
Chebotareva, Natalia A.
Tugaeva, Kristina V.
Kurganov, Boris I.
author_sort Eronina, Tatiana B.
collection PubMed
description 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 (AC(0)) 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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spelling pubmed-89986552022-04-12 Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b Eronina, Tatiana B. Mikhaylova, Valeriya V. Chebotareva, Natalia A. Tugaeva, Kristina V. Kurganov, Boris I. Int J Mol Sci Article 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 (AC(0)) 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. MDPI 2022-03-30 /pmc/articles/PMC8998655/ /pubmed/35409175 http://dx.doi.org/10.3390/ijms23073816 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Eronina, Tatiana B.
Mikhaylova, Valeriya V.
Chebotareva, Natalia A.
Tugaeva, Kristina V.
Kurganov, Boris I.
Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b
title Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b
title_full Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b
title_fullStr Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b
title_full_unstemmed Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b
title_short Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b
title_sort effect of betaine and arginine on interaction of αb-crystallin with glycogen phosphorylase b
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8998655/
https://www.ncbi.nlm.nih.gov/pubmed/35409175
http://dx.doi.org/10.3390/ijms23073816
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