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Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast
Glucose repression is a key regulatory system controlling the metabolism of non-glucose carbon source in yeast. Glucose represses the utilization of maltose, the most abundant fermentable sugar in lean dough and wort, thereby negatively affecting the fermentation efficiency and product quality of pa...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8204090/ https://www.ncbi.nlm.nih.gov/pubmed/34140941 http://dx.doi.org/10.3389/fmicb.2021.665261 |
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author | Yang, Xu Meng, Lu Lin, Xue Jiang, Huan-Yuan Hu, Xiao-Ping Li, Cong-Fa |
author_facet | Yang, Xu Meng, Lu Lin, Xue Jiang, Huan-Yuan Hu, Xiao-Ping Li, Cong-Fa |
author_sort | Yang, Xu |
collection | PubMed |
description | Glucose repression is a key regulatory system controlling the metabolism of non-glucose carbon source in yeast. Glucose represses the utilization of maltose, the most abundant fermentable sugar in lean dough and wort, thereby negatively affecting the fermentation efficiency and product quality of pasta products and beer. In this study, the focus was on the role of three kinases, Elm1, Tos3, and Sak1, in the maltose metabolism of baker’s yeast in lean dough. The results suggested that the three kinases played different roles in the regulation of the maltose metabolism of baker’s yeast with differential regulations on MAL genes. Elm1 was necessary for the maltose metabolism of baker’s yeast in maltose and maltose-glucose, and the overexpression of ELM1 could enhance the maltose metabolism and lean dough fermentation ability by upregulating the transcription of MALx1 (x is the locus) in maltose and maltose-glucose and MALx2 in maltose. The native level of TOS3 and SAK1 was essential for yeast cells to adapt glucose repression, but the overexpression of TOS3 and SAK1 alone repressed the expression of MALx1 in maltose-glucose and MALx2 in maltose. Moreover, the three kinases might regulate the maltose metabolism via the Snf1-parallel pathways with a carbon source-dependent manner. These results, for the first time, suggested that Elm1, rather than Tos3 and Sak1, might be the dominant regulator in the maltose metabolism of baker’s yeast. These findings provided knowledge about the glucose repression of maltose and gave a new perspective for breeding industrial yeasts with rapid maltose metabolism. |
format | Online Article Text |
id | pubmed-8204090 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-82040902021-06-16 Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast Yang, Xu Meng, Lu Lin, Xue Jiang, Huan-Yuan Hu, Xiao-Ping Li, Cong-Fa Front Microbiol Microbiology Glucose repression is a key regulatory system controlling the metabolism of non-glucose carbon source in yeast. Glucose represses the utilization of maltose, the most abundant fermentable sugar in lean dough and wort, thereby negatively affecting the fermentation efficiency and product quality of pasta products and beer. In this study, the focus was on the role of three kinases, Elm1, Tos3, and Sak1, in the maltose metabolism of baker’s yeast in lean dough. The results suggested that the three kinases played different roles in the regulation of the maltose metabolism of baker’s yeast with differential regulations on MAL genes. Elm1 was necessary for the maltose metabolism of baker’s yeast in maltose and maltose-glucose, and the overexpression of ELM1 could enhance the maltose metabolism and lean dough fermentation ability by upregulating the transcription of MALx1 (x is the locus) in maltose and maltose-glucose and MALx2 in maltose. The native level of TOS3 and SAK1 was essential for yeast cells to adapt glucose repression, but the overexpression of TOS3 and SAK1 alone repressed the expression of MALx1 in maltose-glucose and MALx2 in maltose. Moreover, the three kinases might regulate the maltose metabolism via the Snf1-parallel pathways with a carbon source-dependent manner. These results, for the first time, suggested that Elm1, rather than Tos3 and Sak1, might be the dominant regulator in the maltose metabolism of baker’s yeast. These findings provided knowledge about the glucose repression of maltose and gave a new perspective for breeding industrial yeasts with rapid maltose metabolism. Frontiers Media S.A. 2021-06-01 /pmc/articles/PMC8204090/ /pubmed/34140941 http://dx.doi.org/10.3389/fmicb.2021.665261 Text en Copyright © 2021 Yang, Meng, Lin, Jiang, Hu and Li. https://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 Yang, Xu Meng, Lu Lin, Xue Jiang, Huan-Yuan Hu, Xiao-Ping Li, Cong-Fa Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast |
title | Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast |
title_full | Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast |
title_fullStr | Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast |
title_full_unstemmed | Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast |
title_short | Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker’s Yeast |
title_sort | role of elm1, tos3, and sak1 protein kinases in the maltose metabolism of baker’s yeast |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8204090/ https://www.ncbi.nlm.nih.gov/pubmed/34140941 http://dx.doi.org/10.3389/fmicb.2021.665261 |
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