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

Summary 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 methyltra...

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Bibliographic Details
Published in:Molecular microbiology 2012-06, Vol.84 (6), p.1150-1164
Main Authors: 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.
Format: Article
Language:English
Subjects:
Bacteria
Biological and medical sciences
Cellulase - biosynthesis
Cellulose
Chromatin
Fundamental and applied biological sciences. Psychology
Gene Expression
Gene Expression Regulation, Fungal
Microbiology
Miscellaneous
Molecular Sequence Data
Mycology
Protein Methyltransferases - metabolism
Proteins
Sequence Analysis, DNA
Trichoderma - enzymology
Trichoderma - genetics
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Summary:Summary 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.
ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2012.08083.x