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Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction

The signaling of cytokinins (CKs), classical plant hormones, is based on the interaction of proteins that constitute the multistep phosphorelay system (MSP): catalytic receptors—sensor histidine kinases (HKs), phosphotransmitters (HPts), and transcription factors—response regulators (RRs). Any CK re...

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Autores principales: Arkhipov, Dmitry V., Lomin, Sergey N., Myakushina, Yulia A., Savelieva, Ekaterina M., Osolodkin, Dmitry I., Romanov, Georgy A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6539988/
https://www.ncbi.nlm.nih.gov/pubmed/31035389
http://dx.doi.org/10.3390/ijms20092096
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author Arkhipov, Dmitry V.
Lomin, Sergey N.
Myakushina, Yulia A.
Savelieva, Ekaterina M.
Osolodkin, Dmitry I.
Romanov, Georgy A.
author_facet Arkhipov, Dmitry V.
Lomin, Sergey N.
Myakushina, Yulia A.
Savelieva, Ekaterina M.
Osolodkin, Dmitry I.
Romanov, Georgy A.
author_sort Arkhipov, Dmitry V.
collection PubMed
description The signaling of cytokinins (CKs), classical plant hormones, is based on the interaction of proteins that constitute the multistep phosphorelay system (MSP): catalytic receptors—sensor histidine kinases (HKs), phosphotransmitters (HPts), and transcription factors—response regulators (RRs). Any CK receptor was shown to interact in vivo with any of the studied HPts and vice versa. In addition, both of these proteins tend to form a homodimer or a heterodimeric complex with protein-paralog. Our study was aimed at explaining by molecular modeling the observed features of in planta protein–protein interactions, accompanying CK signaling. For this purpose, models of CK-signaling proteins’ structure from Arabidopsis and potato were built. The modeled interaction interfaces were formed by rather conserved areas of protein surfaces, complementary in hydrophobicity and electrostatic potential. Hot spots amino acids, determining specificity and strength of the interaction, were identified. Virtual phosphorylation of conserved Asp or His residues affected this complementation, increasing (Asp-P in HK) or decreasing (His-P in HPt) the affinity of interacting proteins. The HK–HPt and HPt–HPt interfaces overlapped, sharing some of the hot spots. MSP proteins from Arabidopsis and potato exhibited similar properties. The structural features of the modeled protein complexes were consistent with the experimental data.
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spelling pubmed-65399882019-06-04 Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction Arkhipov, Dmitry V. Lomin, Sergey N. Myakushina, Yulia A. Savelieva, Ekaterina M. Osolodkin, Dmitry I. Romanov, Georgy A. Int J Mol Sci Article The signaling of cytokinins (CKs), classical plant hormones, is based on the interaction of proteins that constitute the multistep phosphorelay system (MSP): catalytic receptors—sensor histidine kinases (HKs), phosphotransmitters (HPts), and transcription factors—response regulators (RRs). Any CK receptor was shown to interact in vivo with any of the studied HPts and vice versa. In addition, both of these proteins tend to form a homodimer or a heterodimeric complex with protein-paralog. Our study was aimed at explaining by molecular modeling the observed features of in planta protein–protein interactions, accompanying CK signaling. For this purpose, models of CK-signaling proteins’ structure from Arabidopsis and potato were built. The modeled interaction interfaces were formed by rather conserved areas of protein surfaces, complementary in hydrophobicity and electrostatic potential. Hot spots amino acids, determining specificity and strength of the interaction, were identified. Virtual phosphorylation of conserved Asp or His residues affected this complementation, increasing (Asp-P in HK) or decreasing (His-P in HPt) the affinity of interacting proteins. The HK–HPt and HPt–HPt interfaces overlapped, sharing some of the hot spots. MSP proteins from Arabidopsis and potato exhibited similar properties. The structural features of the modeled protein complexes were consistent with the experimental data. MDPI 2019-04-28 /pmc/articles/PMC6539988/ /pubmed/31035389 http://dx.doi.org/10.3390/ijms20092096 Text en © 2019 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Arkhipov, Dmitry V.
Lomin, Sergey N.
Myakushina, Yulia A.
Savelieva, Ekaterina M.
Osolodkin, Dmitry I.
Romanov, Georgy A.
Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction
title Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction
title_full Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction
title_fullStr Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction
title_full_unstemmed Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction
title_short Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction
title_sort modeling of protein–protein interactions in cytokinin signal transduction
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6539988/
https://www.ncbi.nlm.nih.gov/pubmed/31035389
http://dx.doi.org/10.3390/ijms20092096
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