Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus

Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus

Most mushrooms are thermo-sensitive to temperatures over 23°C, which greatly restricts their agricultural cultivation. Understanding mushroom’s innate heat-tolerance mechanisms may facilitate genetic improvements of their thermotolerance. Agaricus bisporus strain 02 is a relatively thermotolerant mu...

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Main Authors: Lu, Zhonglei, Kong, Xiangxiang, Lu, Zhaoming, Xiao, Meixiang, Chen, Meiyuan, Zhu, Liang, Shen, Yuemao, Hu, Xiangyang, Song, Siyang
Format: Online
Language:English
Published: Public Library of Science 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948851/
id pubmed-3948851
recordtype oai_dc
spelling pubmed-39488512014-03-13 Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus Lu, Zhonglei Kong, Xiangxiang Lu, Zhaoming Xiao, Meixiang Chen, Meiyuan Zhu, Liang Shen, Yuemao Hu, Xiangyang Song, Siyang Research Article Most mushrooms are thermo-sensitive to temperatures over 23°C, which greatly restricts their agricultural cultivation. Understanding mushroom’s innate heat-tolerance mechanisms may facilitate genetic improvements of their thermotolerance. Agaricus bisporus strain 02 is a relatively thermotolerant mushroom strain, while strain 8213 is quite thermo-sensitive. Here, we compared their responses at proteomic level to heat treatment at 33°C. We identified 73 proteins that are differentially expressed between 02 and 8213 or induced upon heat stress in strain 02 itself, 48 of which with a known identity. Among them, 4 proteins are constitutively more highly expressed in 02 than 8213; and they can be further upregulated in response to heat stress in 02, but not in 8213. One protein is encoded by the para-aminobenzoic acid (PABA) synthase gene Pabs, which has been shown to scavenge the reactive oxygen species in vitro. Pabs mRNA and its chemical product PABA show similar heat stress induction pattern as PABA synthase protein and are more abundant in 02, indicating transcriptional level upregulation of Pabs upon heat stress. A specific inhibitor of PABA synthesis impaired thermotolerance of 02, while exogenous PABA or transgenic overexpression of 02 derived PABA synthase enhanced thermotolerance of 8213. Furthermore, compared to 8213, 02 accumulated less H2O2 but more defense-related proteins (e.g., HSPs and Chitinase) under heat stress. Together, these results demonstrate a role of PABA in enhancing mushroom thermotolerance by removing H2O2 and elevating defense-related proteins. Public Library of Science 2014-03-10 /pmc/articles/PMC3948851/ /pubmed/24614118 http://dx.doi.org/10.1371/journal.pone.0091298 Text en © 2014 Lu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lu, Zhonglei
Kong, Xiangxiang
Lu, Zhaoming
Xiao, Meixiang
Chen, Meiyuan
Zhu, Liang
Shen, Yuemao
Hu, Xiangyang
Song, Siyang
spellingShingle Lu, Zhonglei
Kong, Xiangxiang
Lu, Zhaoming
Xiao, Meixiang
Chen, Meiyuan
Zhu, Liang
Shen, Yuemao
Hu, Xiangyang
Song, Siyang
Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus
author_facet Lu, Zhonglei
Kong, Xiangxiang
Lu, Zhaoming
Xiao, Meixiang
Chen, Meiyuan
Zhu, Liang
Shen, Yuemao
Hu, Xiangyang
Song, Siyang
author_sort Lu, Zhonglei
title Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus
title_short Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus
title_full Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus
title_fullStr Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus
title_full_unstemmed Para-Aminobenzoic Acid (PABA) Synthase Enhances Thermotolerance of Mushroom Agaricus bisporus
title_sort para-aminobenzoic acid (paba) synthase enhances thermotolerance of mushroom agaricus bisporus
description Most mushrooms are thermo-sensitive to temperatures over 23°C, which greatly restricts their agricultural cultivation. Understanding mushroom’s innate heat-tolerance mechanisms may facilitate genetic improvements of their thermotolerance. Agaricus bisporus strain 02 is a relatively thermotolerant mushroom strain, while strain 8213 is quite thermo-sensitive. Here, we compared their responses at proteomic level to heat treatment at 33°C. We identified 73 proteins that are differentially expressed between 02 and 8213 or induced upon heat stress in strain 02 itself, 48 of which with a known identity. Among them, 4 proteins are constitutively more highly expressed in 02 than 8213; and they can be further upregulated in response to heat stress in 02, but not in 8213. One protein is encoded by the para-aminobenzoic acid (PABA) synthase gene Pabs, which has been shown to scavenge the reactive oxygen species in vitro. Pabs mRNA and its chemical product PABA show similar heat stress induction pattern as PABA synthase protein and are more abundant in 02, indicating transcriptional level upregulation of Pabs upon heat stress. A specific inhibitor of PABA synthesis impaired thermotolerance of 02, while exogenous PABA or transgenic overexpression of 02 derived PABA synthase enhanced thermotolerance of 8213. Furthermore, compared to 8213, 02 accumulated less H2O2 but more defense-related proteins (e.g., HSPs and Chitinase) under heat stress. Together, these results demonstrate a role of PABA in enhancing mushroom thermotolerance by removing H2O2 and elevating defense-related proteins.
publisher Public Library of Science
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948851/
_version_ 1612066214628032512

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