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Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea
Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. However, the extent of this PTM in non-histone proteins remains unknown. Here, we report the first proteomic survey of this modification i...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7649125/ https://www.ncbi.nlm.nih.gov/pubmed/33193272 http://dx.doi.org/10.3389/fmicb.2020.594743 |
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author | Gao, Mingming Zhang, Ning Liang, Wenxing |
author_facet | Gao, Mingming Zhang, Ning Liang, Wenxing |
author_sort | Gao, Mingming |
collection | PubMed |
description | Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. However, the extent of this PTM in non-histone proteins remains unknown. Here, we report the first proteomic survey of this modification in Botrytis cinerea, a destructive necrotrophic fungal pathogen distributed worldwide. After a global lysine lactylome analysis using LC-MS/MS, we identified 273 Kla sites in 166 proteins, of which contained in 4 types of modification motifs. Our results show that the majority of lactylated proteins were distributed in nucleus (36%), mitochondria (27%), and cytoplasm (25%). The identified proteins were found to be involved in diverse cellular processes. Most strikingly, Kla was found in 43 structural constituent proteins of ribosome, indicating an impact of Kla in protein synthesis. Moreover, 12 lactylated proteins participated in fungal pathogenicity, suggesting a potential role for Kla in this process. Protein interaction network analysis suggested that a mass of protein interactions are regulated by lactylation. The combined data sets represent the first report of the lactylome of B. cinerea and provide a good foundation for further explorations of Kla in plant fungal pathogens. |
format | Online Article Text |
id | pubmed-7649125 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-76491252020-11-13 Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea Gao, Mingming Zhang, Ning Liang, Wenxing Front Microbiol Microbiology Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. However, the extent of this PTM in non-histone proteins remains unknown. Here, we report the first proteomic survey of this modification in Botrytis cinerea, a destructive necrotrophic fungal pathogen distributed worldwide. After a global lysine lactylome analysis using LC-MS/MS, we identified 273 Kla sites in 166 proteins, of which contained in 4 types of modification motifs. Our results show that the majority of lactylated proteins were distributed in nucleus (36%), mitochondria (27%), and cytoplasm (25%). The identified proteins were found to be involved in diverse cellular processes. Most strikingly, Kla was found in 43 structural constituent proteins of ribosome, indicating an impact of Kla in protein synthesis. Moreover, 12 lactylated proteins participated in fungal pathogenicity, suggesting a potential role for Kla in this process. Protein interaction network analysis suggested that a mass of protein interactions are regulated by lactylation. The combined data sets represent the first report of the lactylome of B. cinerea and provide a good foundation for further explorations of Kla in plant fungal pathogens. Frontiers Media S.A. 2020-10-26 /pmc/articles/PMC7649125/ /pubmed/33193272 http://dx.doi.org/10.3389/fmicb.2020.594743 Text en Copyright © 2020 Gao, Zhang and Liang. 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 Gao, Mingming Zhang, Ning Liang, Wenxing Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea |
title | Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea |
title_full | Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea |
title_fullStr | Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea |
title_full_unstemmed | Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea |
title_short | Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea |
title_sort | systematic analysis of lysine lactylation in the plant fungal pathogen botrytis cinerea |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7649125/ https://www.ncbi.nlm.nih.gov/pubmed/33193272 http://dx.doi.org/10.3389/fmicb.2020.594743 |
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