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

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https://ir.library.oregonstate.edu/concern/articles/rx913q57p

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  • 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.
  • This is the publisher’s final pdf. The published article is copyrighted by Wiley-Blackwell and can be found at: http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958/issues
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  • Seiboth, B., Karimi, R. A., Phatale, P. A., Linke, R., Hartl, L., Sauer, D. G., Smith, K. M., Baker, S. E., Freitag, M. and Kubicek, C. P. (2012), The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei. Molecular Microbiology, 84: 1150–1164. doi: 10.1111/j.1365-2958.2012.08083.x
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  • 84
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  • 6
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  • This study was supported by a grant of the Austrian Science Foundation to C.P.K. (P 21266), funds from the OSU Computational and Genome Biology Initiative and PNNL to M.F. K.M.S. was supported by funds from an NIH grant (P01GM068087).
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file details PhatalePallaviBiochemBiophysPutativeProteinMethyltransferase.pdf 2017-07-10 Öffentlich Herunterladen