2020
DOI: 10.1371/journal.pgen.1008979
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Trichoderma reesei XYR1 activates cellulase gene expression via interaction with the Mediator subunit TrGAL11 to recruit RNA polymerase II

Abstract: The ascomycete Trichoderma reesei is a highly prolific cellulase producer. While XYR1 (Xylanase regulator 1) has been firmly established to be the master activator of cellulase gene expression in T. reesei, its precise transcriptional activation mechanism remains poorly understood. In the present study, TrGAL11, a component of the Mediator tail module, was identified as a putative interacting partner of XYR1. Deletion of Trgal11 markedly impaired the induced expression of most (hemi)cellulase genes, but not th… Show more

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Cited by 23 publications
(14 citation statements)
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“…DEGs related to DNA metabolism were found, like DNA topoisomerase IV alpha subunit, and DNase I protein. In particular, 14 DEGs are specifically involved in regulation of transcription by RNA polymerase II that is responsible for the transcription of cellulase production [ 67 ]. On the other hand, three tRNA were downregulated, including tRNA-Arg, tRNA-Glu and tRNA-Lys, while threonyl/alanyl tRNA synthetase and eukaryotic translation initiation factor 2c were upregulated.…”
Section: Resultsmentioning
confidence: 99%
“…DEGs related to DNA metabolism were found, like DNA topoisomerase IV alpha subunit, and DNase I protein. In particular, 14 DEGs are specifically involved in regulation of transcription by RNA polymerase II that is responsible for the transcription of cellulase production [ 67 ]. On the other hand, three tRNA were downregulated, including tRNA-Arg, tRNA-Glu and tRNA-Lys, while threonyl/alanyl tRNA synthetase and eukaryotic translation initiation factor 2c were upregulated.…”
Section: Resultsmentioning
confidence: 99%
“…In addition to these genes, transcription factors also play an irreplaceable role in this process. Recent studies in T. reesei found Xyr1 in functions as the central regulator of cellulases to control the expression of CAZyme genes by interacting with TrGAL11 [33]. However, the expression of xyr1 was negatively regulated by the CCR proteins Cre1 and Ace1 [34].…”
Section: Discussionmentioning
confidence: 99%
“…Regardless of this, given the multiple protein interaction sites on CYC8/TUP1 and its significant potential of being incorporated in different complexes [ 15 19 ], it is reasonable to anticipate that the way by which CYC8/TUP1 achieves its repression may also apply to its activation. Our previous results demonstrate that XYR1 directly interacts with SWI/SNF and the Mediator tail subunit to facilitate the recruitment of the general transcription machinery including RNA Pol II to successfully initiate the transcription of these cellulase genes [ 49 , 50 ]. One possibility is thus that, upon recruited by XYR1, the TrCYC8/TUP1 complex cooperates with XYR1 to achieve the efficient recruitment of the above components allowing the rapid and high-level cellulase gene activation.…”
Section: Discussionmentioning
confidence: 99%
“…The reaction was stopped by addition of 50 μl of 10% Na 2 CO 3 solution. One unit (U) of p NPCase or p NPGase activity is defined as the amount of enzyme releasing 1 μmol of p NP per minute [ 49 ]. SDS-PAGE and western blotting were performed according to standard protocols and CEL7A (CBH1) was immunoblotted using a polyclonal antibody raised against amino acids 426–446 of the protein, as previously described [ 55 ].…”
Section: Methodsmentioning
confidence: 99%
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