{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhao Q"],"funding":["China National Tobacco Corp","China National Tobacco Corporation","Ministry of Science and Technology of the People&apos;s Republic of China","National Natural Science Foundation of China","National Key Research and Development Program of China"],"pagination":["732-740"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10770280"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(4)"],"pubmed_abstract":["The filamentous fungus <i>Trichoderma reesei</i> is widely used for the production of lignocellulolytic enzymes in industry. XYR1 is the major transcriptional activator of cellulases and hemicellulases in <i>T. reesei</i>. However, rational engineering of XYR1 for improved lignocellulolytic enzymes production has been limited by the lack of structure information. Here, alanine 873 was identified as a new potential target for the engineering of XYR1 based on its structure predicted by AlphaFold2. The mutation of this residue to tyrosine enabled significantly enhanced production of xylanolytic enzymes in the medium with cellulose as the carbon source. Moreover, xylanase and cellulase production increased by 56.7- and 3.3-fold, respectively, when glucose was used as the sole carbon source. Un"],"journal":["Synthetic and systems biotechnology"],"pubmed_title":["Structure-guided engineering of transcriptional activator XYR1 for inducer-free production of lignocellulolytic enzymes in <i>Trichoderma reesei</i>."],"pmcid":["PMC10770280"],"funding_grant_id":["2018YFA0900500","32170037","110202102018"],"pubmed_authors":["Xing J","Yang Z","Zhang Z","Liang H","Zhao Q","Xiao Z","Gao L","Qu Y","Zhao J","Liu G"],"additional_accession":[]},"is_claimable":false,"name":"Structure-guided engineering of transcriptional activator XYR1 for inducer-free production of lignocellulolytic enzymes in <i>Trichoderma reesei</i>.","description":"The filamentous fungus <i>Trichoderma reesei</i> is widely used for the production of lignocellulolytic enzymes in industry. XYR1 is the major transcriptional activator of cellulases and hemicellulases in <i>T. reesei</i>. However, rational engineering of XYR1 for improved lignocellulolytic enzymes production has been limited by the lack of structure information. Here, alanine 873 was identified as a new potential target for the engineering of XYR1 based on its structure predicted by AlphaFold2. The mutation of this residue to tyrosine enabled significantly enhanced production of xylanolytic enzymes in the medium with cellulose as the carbon source. Moreover, xylanase and cellulase production increased by 56.7- and 3.3-fold, respectively, when glucose was used as the sole carbon source. Un","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2026-07-15T08:27:09.859Z","creation":"2025-04-06T13:11:16.659Z"},"accession":"S-EPMC10770280","cross_references":{"pubmed":["38187093"],"doi":["10.1016/j.synbio.2023.11.005"]}}