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Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei
Trichoderma reesei represents one of the most prolific producers of plant cell wall degrading enzymes. Recent research showed broad regulation by phosphorylation in T. reesei, including important transcription factors involved in cellulase regulation. To evaluate factors crucial for changes in these...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6662751/ https://www.ncbi.nlm.nih.gov/pubmed/31358805 http://dx.doi.org/10.1038/s41598-019-47421-z |
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author | Rodriguez-Iglesias, Aroa Schmoll, Monika |
author_facet | Rodriguez-Iglesias, Aroa Schmoll, Monika |
author_sort | Rodriguez-Iglesias, Aroa |
collection | PubMed |
description | Trichoderma reesei represents one of the most prolific producers of plant cell wall degrading enzymes. Recent research showed broad regulation by phosphorylation in T. reesei, including important transcription factors involved in cellulase regulation. To evaluate factors crucial for changes in these phosphorylation events, we studied non-essential protein phosphatases (PPs) of T. reesei. Viable deletion strains were tested for growth on different carbon sources, osmotic and oxidative stress response, asexual and sexual development, cellulase and protease production as well as secondary metabolism. Six PPs were found to be positive or negative regulators for cellulase production. A correlation of the effects of PPs on protease activities and cellulase activities was not detected. Hierarchical clustering of regulation patterns and phenotypes of deletion indicated functional specialization within PP classes and common as well as variable effects. Our results confirmed the central role of catalytic and regulatory subunits of PP2A which regulates several aspects of cell growth and metabolism. Moreover we show that the additional homologue of PPH5 in Trichoderma spp., PPH5-2 assumes distinct functions in metabolism, development and stress response, different from PPH5. The influence of PPs on both cellulase gene expression and secondary metabolite production support an interrelationship in the underlying regulation mechanisms. |
format | Online Article Text |
id | pubmed-6662751 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-66627512019-08-02 Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei Rodriguez-Iglesias, Aroa Schmoll, Monika Sci Rep Article Trichoderma reesei represents one of the most prolific producers of plant cell wall degrading enzymes. Recent research showed broad regulation by phosphorylation in T. reesei, including important transcription factors involved in cellulase regulation. To evaluate factors crucial for changes in these phosphorylation events, we studied non-essential protein phosphatases (PPs) of T. reesei. Viable deletion strains were tested for growth on different carbon sources, osmotic and oxidative stress response, asexual and sexual development, cellulase and protease production as well as secondary metabolism. Six PPs were found to be positive or negative regulators for cellulase production. A correlation of the effects of PPs on protease activities and cellulase activities was not detected. Hierarchical clustering of regulation patterns and phenotypes of deletion indicated functional specialization within PP classes and common as well as variable effects. Our results confirmed the central role of catalytic and regulatory subunits of PP2A which regulates several aspects of cell growth and metabolism. Moreover we show that the additional homologue of PPH5 in Trichoderma spp., PPH5-2 assumes distinct functions in metabolism, development and stress response, different from PPH5. The influence of PPs on both cellulase gene expression and secondary metabolite production support an interrelationship in the underlying regulation mechanisms. Nature Publishing Group UK 2019-07-29 /pmc/articles/PMC6662751/ /pubmed/31358805 http://dx.doi.org/10.1038/s41598-019-47421-z Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Rodriguez-Iglesias, Aroa Schmoll, Monika Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei |
title | Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei |
title_full | Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei |
title_fullStr | Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei |
title_full_unstemmed | Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei |
title_short | Protein phosphatases regulate growth, development, cellulases and secondary metabolism in Trichoderma reesei |
title_sort | protein phosphatases regulate growth, development, cellulases and secondary metabolism in trichoderma reesei |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6662751/ https://www.ncbi.nlm.nih.gov/pubmed/31358805 http://dx.doi.org/10.1038/s41598-019-47421-z |
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