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Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis
The Med1 transcriptional coactivator is a crucial component of the Mediator middle complex, which regulates the expression of specific genes involved in cell development, differentiation, reproduction, and homeostasis. The Med1 LxxLL motif, a five-amino-acid peptide sequence, is essential for Med1-m...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10675092/ https://www.ncbi.nlm.nih.gov/pubmed/37999515 http://dx.doi.org/10.3390/toxins15110652 |
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author | Zhou, Zehua Liu, Jie Zhang, Jie Yan, Huijuan Yi, Tuyong Shim, Won Bo |
author_facet | Zhou, Zehua Liu, Jie Zhang, Jie Yan, Huijuan Yi, Tuyong Shim, Won Bo |
author_sort | Zhou, Zehua |
collection | PubMed |
description | The Med1 transcriptional coactivator is a crucial component of the Mediator middle complex, which regulates the expression of specific genes involved in cell development, differentiation, reproduction, and homeostasis. The Med1 LxxLL motif, a five-amino-acid peptide sequence, is essential for Med1-mediated gene expression. Our previous study revealed that the disruption of the Med1 subunit leads to a significant increase in fumonisin B(1) (FB(1)) production in the maize pathogen Fusarium verticillioides. However, our understanding of how Med1 regulates FB(1) biosynthesis in F. verticillioides, particularly through the Med1 LxxLL motifs, remains limited. To characterize the role of LxxLL motifs, we generated a series of Med1 LxxLL deletion and amino acid substitution mutants. These mutants exhibited impaired mycelial growth and conidia germination while demonstrating enhanced conidia production and virulence. Similar to the Med1 deletion mutant, Med1 LxxLL motif mutants also exhibited increased FB(1) biosynthesis in F. verticillioides. Proteomic profiling revealed that the Med1 LxxLL motif regulated the biosynthesis of several key substances that affected FB(1) production, including starch and carotenoid. Subsequent studies demonstrated that the production of amylopectin, which is strongly linked to FB(1) biosynthesis, was significantly increased in Med1 LxxLL motif mutants. In addition, the disruption of carotenoid metabolic genes decreased carotenoid content, thus stimulating FB(1) biosynthesis in F. verticillioides. Taken together, our results provide valuable insights into how the Med1 LxxLL motif regulates FB(1) biosynthesis in the mycotoxigenic fungus F. verticillioides. |
format | Online Article Text |
id | pubmed-10675092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106750922023-11-13 Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis Zhou, Zehua Liu, Jie Zhang, Jie Yan, Huijuan Yi, Tuyong Shim, Won Bo Toxins (Basel) Article The Med1 transcriptional coactivator is a crucial component of the Mediator middle complex, which regulates the expression of specific genes involved in cell development, differentiation, reproduction, and homeostasis. The Med1 LxxLL motif, a five-amino-acid peptide sequence, is essential for Med1-mediated gene expression. Our previous study revealed that the disruption of the Med1 subunit leads to a significant increase in fumonisin B(1) (FB(1)) production in the maize pathogen Fusarium verticillioides. However, our understanding of how Med1 regulates FB(1) biosynthesis in F. verticillioides, particularly through the Med1 LxxLL motifs, remains limited. To characterize the role of LxxLL motifs, we generated a series of Med1 LxxLL deletion and amino acid substitution mutants. These mutants exhibited impaired mycelial growth and conidia germination while demonstrating enhanced conidia production and virulence. Similar to the Med1 deletion mutant, Med1 LxxLL motif mutants also exhibited increased FB(1) biosynthesis in F. verticillioides. Proteomic profiling revealed that the Med1 LxxLL motif regulated the biosynthesis of several key substances that affected FB(1) production, including starch and carotenoid. Subsequent studies demonstrated that the production of amylopectin, which is strongly linked to FB(1) biosynthesis, was significantly increased in Med1 LxxLL motif mutants. In addition, the disruption of carotenoid metabolic genes decreased carotenoid content, thus stimulating FB(1) biosynthesis in F. verticillioides. Taken together, our results provide valuable insights into how the Med1 LxxLL motif regulates FB(1) biosynthesis in the mycotoxigenic fungus F. verticillioides. MDPI 2023-11-13 /pmc/articles/PMC10675092/ /pubmed/37999515 http://dx.doi.org/10.3390/toxins15110652 Text en © 2023 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 Zhou, Zehua Liu, Jie Zhang, Jie Yan, Huijuan Yi, Tuyong Shim, Won Bo Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis |
title | Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis |
title_full | Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis |
title_fullStr | Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis |
title_full_unstemmed | Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis |
title_short | Characterization of Fusarium verticillioides Med1 LxxLL Motif Involved in Fumonisin Biosynthesis |
title_sort | characterization of fusarium verticillioides med1 lxxll motif involved in fumonisin biosynthesis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10675092/ https://www.ncbi.nlm.nih.gov/pubmed/37999515 http://dx.doi.org/10.3390/toxins15110652 |
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