Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i>
Morels (<i>Morchella</i> spp.), as one of the rare macroascomycetes that can be cultivated artificially, possess significant economic and scientific values. Morel cultivation is highly sensitive to elevated temperatures; however, the mechanisms of their response to heat shock remain poor...
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2025-01-01
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author | Jiexiong Zhang Yanxia Li Yifan Mao Yesheng Zhang Botong Zhou Wei Liu Wen Wang Chen Zhang |
author_facet | Jiexiong Zhang Yanxia Li Yifan Mao Yesheng Zhang Botong Zhou Wei Liu Wen Wang Chen Zhang |
author_sort | Jiexiong Zhang |
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description | Morels (<i>Morchella</i> spp.), as one of the rare macroascomycetes that can be cultivated artificially, possess significant economic and scientific values. Morel cultivation is highly sensitive to elevated temperatures; however, the mechanisms of their response to heat shock remain poorly understood. This study integrated transcriptomic and quantitative proteomic analyses of two <i>M. sextelata</i> strains with different thermotolerance (labeled as strains C and D) under normal (18 °C) and high temperature (28 °C) conditions. From over 9300 transcripts and 5000 proteins, both consistency and heterogeneity were found in response to heat shock between the two strains. Both strains displayed a capacity to maintain cellular homeostasis in response to heat shock through highly expressed cell wall integrity (CWI) pathways, heat shock proteins (HSPs), and antioxidant systems. However, strain D, which exhibited stronger thermotolerance, specifically upregulated the ubiquitin ligase <i>Rsp5</i>, thereby further promoting the expression of HSPs, which may be a key factor influencing the thermotolerance difference among <i>M. sextelata</i> strains. A conceptual model of the heat shock adaptation regulatory network in <i>M. sextelata</i> was proposed for the first time; the results provide novel insights into the thermotolerance response mechanisms of macroascomycetes and valuable resources for the breeding enhancement of thermotolerant morel strains. |
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spelling | doaj-art-45383c8f555c455bb5119bc6cac94f672025-01-24T13:37:27ZengMDPI AGJournal of Fungi2309-608X2025-01-011117610.3390/jof11010076Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i>Jiexiong Zhang0Yanxia Li1Yifan Mao2Yesheng Zhang3Botong Zhou4Wei Liu5Wen Wang6Chen Zhang7School of Ecology and Environment, Northwestern Polytechnical University, Xi’an 710072, ChinaShandong Junsheng Biotechnologies Co., Ltd., Liaocheng 252400, ChinaSchool of Ecology and Environment, Northwestern Polytechnical University, Xi’an 710072, ChinaShandong Junsheng Biotechnologies Co., Ltd., Liaocheng 252400, ChinaSchool of Ecology and Environment, Northwestern Polytechnical University, Xi’an 710072, ChinaThe Germplasm Bank of Wild Species, Yunnan Key Laboratory for Fungal Diversity and Green Development, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, ChinaSchool of Ecology and Environment, Northwestern Polytechnical University, Xi’an 710072, ChinaSchool of Ecology and Environment, Northwestern Polytechnical University, Xi’an 710072, ChinaMorels (<i>Morchella</i> spp.), as one of the rare macroascomycetes that can be cultivated artificially, possess significant economic and scientific values. Morel cultivation is highly sensitive to elevated temperatures; however, the mechanisms of their response to heat shock remain poorly understood. This study integrated transcriptomic and quantitative proteomic analyses of two <i>M. sextelata</i> strains with different thermotolerance (labeled as strains C and D) under normal (18 °C) and high temperature (28 °C) conditions. From over 9300 transcripts and 5000 proteins, both consistency and heterogeneity were found in response to heat shock between the two strains. Both strains displayed a capacity to maintain cellular homeostasis in response to heat shock through highly expressed cell wall integrity (CWI) pathways, heat shock proteins (HSPs), and antioxidant systems. However, strain D, which exhibited stronger thermotolerance, specifically upregulated the ubiquitin ligase <i>Rsp5</i>, thereby further promoting the expression of HSPs, which may be a key factor influencing the thermotolerance difference among <i>M. sextelata</i> strains. A conceptual model of the heat shock adaptation regulatory network in <i>M. sextelata</i> was proposed for the first time; the results provide novel insights into the thermotolerance response mechanisms of macroascomycetes and valuable resources for the breeding enhancement of thermotolerant morel strains.https://www.mdpi.com/2309-608X/11/1/76thermotolerance<i>Morchella sextelata</i>CWIHSPsantioxidantribosome |
spellingShingle | Jiexiong Zhang Yanxia Li Yifan Mao Yesheng Zhang Botong Zhou Wei Liu Wen Wang Chen Zhang Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i> Journal of Fungi thermotolerance <i>Morchella sextelata</i> CWI HSPs antioxidant ribosome |
title | Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i> |
title_full | Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i> |
title_fullStr | Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i> |
title_full_unstemmed | Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i> |
title_short | Integrated Transcriptomic and Proteomic Analyses Reveal Molecular Mechanism of Response to Heat Shock in <i>Morchella sextelata</i> |
title_sort | integrated transcriptomic and proteomic analyses reveal molecular mechanism of response to heat shock in i morchella sextelata i |
topic | thermotolerance <i>Morchella sextelata</i> CWI HSPs antioxidant ribosome |
url | https://www.mdpi.com/2309-608X/11/1/76 |
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