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Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae

Melatonin is a bioactive compound that is present in fermented beverages and synthesized by yeast during alcoholic fermentation. Many studies have shown that melatonin interacts with some mammalian proteins, such as sirtuins or orphan receptor family proteins. The aim of this study was to determine...

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Autores principales: Morcillo-Parra, María Ángeles, Valera, María José, Beltran, Gemma, Mas, Albert, Torija, María-Jesús
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6821644/
https://www.ncbi.nlm.nih.gov/pubmed/31708896
http://dx.doi.org/10.3389/fmicb.2019.02424
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author Morcillo-Parra, María Ángeles
Valera, María José
Beltran, Gemma
Mas, Albert
Torija, María-Jesús
author_facet Morcillo-Parra, María Ángeles
Valera, María José
Beltran, Gemma
Mas, Albert
Torija, María-Jesús
author_sort Morcillo-Parra, María Ángeles
collection PubMed
description Melatonin is a bioactive compound that is present in fermented beverages and synthesized by yeast during alcoholic fermentation. Many studies have shown that melatonin interacts with some mammalian proteins, such as sirtuins or orphan receptor family proteins. The aim of this study was to determine the intracellular synthesis profile of melatonin in Saccharomyces cerevisiae and to identify the proteins that may interact with this molecule in yeast cells. Melatonin from fermentation samples was analyzed by liquid chromatography mass spectrometry, and proteins bound to melatonin were immunopurified by melatonin-IgG-Dynabeads. Melatonin was produced intracellularly in the lag phase of yeast growth and was exported to the extracellular media during the stationary phase. During this period, melatonin was bound to six proteins with molecular weights from 55 to 35 kDa. Sequence analysis showed that most proteins shared high levels of homology with glycolytic enzymes. An RNA-binding protein was also identified, the elongation alpha factor, which is related to mitochondria. This study reports for the first time the interaction of melatonin and proteins inside yeast cells. These results highlight the possible role of melatonin as a signal molecule and provide a new perspective for understanding its role in yeast.
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spelling pubmed-68216442019-11-08 Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae Morcillo-Parra, María Ángeles Valera, María José Beltran, Gemma Mas, Albert Torija, María-Jesús Front Microbiol Microbiology Melatonin is a bioactive compound that is present in fermented beverages and synthesized by yeast during alcoholic fermentation. Many studies have shown that melatonin interacts with some mammalian proteins, such as sirtuins or orphan receptor family proteins. The aim of this study was to determine the intracellular synthesis profile of melatonin in Saccharomyces cerevisiae and to identify the proteins that may interact with this molecule in yeast cells. Melatonin from fermentation samples was analyzed by liquid chromatography mass spectrometry, and proteins bound to melatonin were immunopurified by melatonin-IgG-Dynabeads. Melatonin was produced intracellularly in the lag phase of yeast growth and was exported to the extracellular media during the stationary phase. During this period, melatonin was bound to six proteins with molecular weights from 55 to 35 kDa. Sequence analysis showed that most proteins shared high levels of homology with glycolytic enzymes. An RNA-binding protein was also identified, the elongation alpha factor, which is related to mitochondria. This study reports for the first time the interaction of melatonin and proteins inside yeast cells. These results highlight the possible role of melatonin as a signal molecule and provide a new perspective for understanding its role in yeast. Frontiers Media S.A. 2019-10-24 /pmc/articles/PMC6821644/ /pubmed/31708896 http://dx.doi.org/10.3389/fmicb.2019.02424 Text en Copyright © 2019 Morcillo-Parra, Valera, Beltran, Mas and Torija. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Morcillo-Parra, María Ángeles
Valera, María José
Beltran, Gemma
Mas, Albert
Torija, María-Jesús
Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae
title Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae
title_full Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae
title_fullStr Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae
title_full_unstemmed Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae
title_short Glycolytic Proteins Interact With Intracellular Melatonin in Saccharomyces cerevisiae
title_sort glycolytic proteins interact with intracellular melatonin in saccharomyces cerevisiae
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6821644/
https://www.ncbi.nlm.nih.gov/pubmed/31708896
http://dx.doi.org/10.3389/fmicb.2019.02424
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