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The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei

Trichoderma reesei is an industrial producer of enzymes that degrade lignocellulosic polysaccharides to soluble monomers, which can be fermented to biofuels. Here we show that the expression of genes for lignocellulose degradation are controlled by the orthologous T. reesei protein methyltransferase...

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Autores principales: Seiboth, Bernhard, Karimi, Razieh Aghcheh, Phatale, Pallavi A, Linke, Rita, Hartl, Lukas, Sauer, Dominik G, Smith, Kristina M, Baker, Scott E, Freitag, Michael, Kubicek, Christian P
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370264/
https://www.ncbi.nlm.nih.gov/pubmed/22554051
http://dx.doi.org/10.1111/j.1365-2958.2012.08083.x
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author Seiboth, Bernhard
Karimi, Razieh Aghcheh
Phatale, Pallavi A
Linke, Rita
Hartl, Lukas
Sauer, Dominik G
Smith, Kristina M
Baker, Scott E
Freitag, Michael
Kubicek, Christian P
author_facet Seiboth, Bernhard
Karimi, Razieh Aghcheh
Phatale, Pallavi A
Linke, Rita
Hartl, Lukas
Sauer, Dominik G
Smith, Kristina M
Baker, Scott E
Freitag, Michael
Kubicek, Christian P
author_sort Seiboth, Bernhard
collection PubMed
description Trichoderma reesei is an industrial producer of enzymes that degrade lignocellulosic polysaccharides to soluble monomers, which can be fermented to biofuels. Here we show that the expression of genes for lignocellulose degradation are controlled by the orthologous T. reesei protein methyltransferase LAE1. In a lae1 deletion mutant we observed a complete loss of expression of all seven cellulases, auxiliary factors for cellulose degradation, β-glucosidases and xylanases were no longer expressed. Conversely, enhanced expression of lae1 resulted in significantly increased cellulase gene transcription. Lae1-modulated cellulase gene expression was dependent on the function of the general cellulase regulator XYR1, but also xyr1 expression was LAE1-dependent. LAE1 was also essential for conidiation of T. reesei. Chromatin immunoprecipitation followed by high-throughput sequencing (‘ChIP-seq’) showed that lae1 expression was not obviously correlated with H3K4 di- or trimethylation (indicative of active transcription) or H3K9 trimethylation (typical for heterochromatin regions) in CAZyme coding regions, suggesting that LAE1 does not affect CAZyme gene expression by directly modulating H3K4 or H3K9 methylation. Our data demonstrate that the putative protein methyltransferase LAE1 is essential for cellulase gene expression in T. reesei through mechanisms that remain to be identified.
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spelling pubmed-33702642012-07-24 The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei Seiboth, Bernhard Karimi, Razieh Aghcheh Phatale, Pallavi A Linke, Rita Hartl, Lukas Sauer, Dominik G Smith, Kristina M Baker, Scott E Freitag, Michael Kubicek, Christian P Mol Microbiol Research Articles Trichoderma reesei is an industrial producer of enzymes that degrade lignocellulosic polysaccharides to soluble monomers, which can be fermented to biofuels. Here we show that the expression of genes for lignocellulose degradation are controlled by the orthologous T. reesei protein methyltransferase LAE1. In a lae1 deletion mutant we observed a complete loss of expression of all seven cellulases, auxiliary factors for cellulose degradation, β-glucosidases and xylanases were no longer expressed. Conversely, enhanced expression of lae1 resulted in significantly increased cellulase gene transcription. Lae1-modulated cellulase gene expression was dependent on the function of the general cellulase regulator XYR1, but also xyr1 expression was LAE1-dependent. LAE1 was also essential for conidiation of T. reesei. Chromatin immunoprecipitation followed by high-throughput sequencing (‘ChIP-seq’) showed that lae1 expression was not obviously correlated with H3K4 di- or trimethylation (indicative of active transcription) or H3K9 trimethylation (typical for heterochromatin regions) in CAZyme coding regions, suggesting that LAE1 does not affect CAZyme gene expression by directly modulating H3K4 or H3K9 methylation. Our data demonstrate that the putative protein methyltransferase LAE1 is essential for cellulase gene expression in T. reesei through mechanisms that remain to be identified. Blackwell Publishing Ltd 2012-06 /pmc/articles/PMC3370264/ /pubmed/22554051 http://dx.doi.org/10.1111/j.1365-2958.2012.08083.x Text en © 2012 Blackwell Publishing Ltd http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Terms and Conditions set out at http://wileyonlinelibrary.com/onlineopen#OnlineOpen_Terms
spellingShingle Research Articles
Seiboth, Bernhard
Karimi, Razieh Aghcheh
Phatale, Pallavi A
Linke, Rita
Hartl, Lukas
Sauer, Dominik G
Smith, Kristina M
Baker, Scott E
Freitag, Michael
Kubicek, Christian P
The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
title The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
title_full The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
title_fullStr The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
title_full_unstemmed The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
title_short The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
title_sort putative protein methyltransferase lae1 controls cellulase gene expression in trichoderma reesei
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370264/
https://www.ncbi.nlm.nih.gov/pubmed/22554051
http://dx.doi.org/10.1111/j.1365-2958.2012.08083.x
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