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CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei

The stringent regulatory network of cellulase gene expression in the filamentous fungus Trichoderma reesei involves multiple transcriptional regulators. However, identification and mechanistic investigation of these regulators are still insufficient. Here, we identified a novel transcriptional regul...

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Autores principales: Wang, Lei, Yang, Renfei, Cao, Yanli, Zheng, Fanglin, Meng, Xiangfeng, Zhong, Yaohua, Chen, Guanjun, Zhang, Weixin, Liu, Weifeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6691364/
https://www.ncbi.nlm.nih.gov/pubmed/31447796
http://dx.doi.org/10.3389/fmicb.2019.01700
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author Wang, Lei
Yang, Renfei
Cao, Yanli
Zheng, Fanglin
Meng, Xiangfeng
Zhong, Yaohua
Chen, Guanjun
Zhang, Weixin
Liu, Weifeng
author_facet Wang, Lei
Yang, Renfei
Cao, Yanli
Zheng, Fanglin
Meng, Xiangfeng
Zhong, Yaohua
Chen, Guanjun
Zhang, Weixin
Liu, Weifeng
author_sort Wang, Lei
collection PubMed
description The stringent regulatory network of cellulase gene expression in the filamentous fungus Trichoderma reesei involves multiple transcriptional regulators. However, identification and mechanistic investigation of these regulators are still insufficient. Here, we identified a novel transcriptional regulator, CLP1, a plant homeo domain (PHD) Protein that participates in regulating T. reesei cellulase gene expression. Phylogenetic analyses demonstrated that CLP1 homologs are widely distributed in filamentous fungi including Trichoderma, Penicillium, Fusarium, Neurospora, and Aspergillus species. We demonstrated that CLP1 is a nuclear protein and lack of CLP1 significantly impaired the induced expression of cellulase genes. ChIP experiments showed CLP1 binding to the cellulase gene promoters specifically under cellulose conditions and compromised XYR1 occupancy on the same promoters in the absence of CLP1 at the early induction stage. XYR1 overexpression fully rescued the defect in cellulase production but not the defect in conidia formation in the clp1 null mutant. Further analysis showed that the PHD is required for the CLP1 appropriate subcellular localization as well as the induced cellulase gene expression and conidiation. Taken together, these data demonstrated an important role of CLP1 in the regulation of cellulase and xylanase gene expression in T. reesei.
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spelling pubmed-66913642019-08-23 CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei Wang, Lei Yang, Renfei Cao, Yanli Zheng, Fanglin Meng, Xiangfeng Zhong, Yaohua Chen, Guanjun Zhang, Weixin Liu, Weifeng Front Microbiol Microbiology The stringent regulatory network of cellulase gene expression in the filamentous fungus Trichoderma reesei involves multiple transcriptional regulators. However, identification and mechanistic investigation of these regulators are still insufficient. Here, we identified a novel transcriptional regulator, CLP1, a plant homeo domain (PHD) Protein that participates in regulating T. reesei cellulase gene expression. Phylogenetic analyses demonstrated that CLP1 homologs are widely distributed in filamentous fungi including Trichoderma, Penicillium, Fusarium, Neurospora, and Aspergillus species. We demonstrated that CLP1 is a nuclear protein and lack of CLP1 significantly impaired the induced expression of cellulase genes. ChIP experiments showed CLP1 binding to the cellulase gene promoters specifically under cellulose conditions and compromised XYR1 occupancy on the same promoters in the absence of CLP1 at the early induction stage. XYR1 overexpression fully rescued the defect in cellulase production but not the defect in conidia formation in the clp1 null mutant. Further analysis showed that the PHD is required for the CLP1 appropriate subcellular localization as well as the induced cellulase gene expression and conidiation. Taken together, these data demonstrated an important role of CLP1 in the regulation of cellulase and xylanase gene expression in T. reesei. Frontiers Media S.A. 2019-08-06 /pmc/articles/PMC6691364/ /pubmed/31447796 http://dx.doi.org/10.3389/fmicb.2019.01700 Text en Copyright © 2019 Wang, Yang, Cao, Zheng, Meng, Zhong, Chen, Zhang and Liu. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Wang, Lei
Yang, Renfei
Cao, Yanli
Zheng, Fanglin
Meng, Xiangfeng
Zhong, Yaohua
Chen, Guanjun
Zhang, Weixin
Liu, Weifeng
CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei
title CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei
title_full CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei
title_fullStr CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei
title_full_unstemmed CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei
title_short CLP1, a Novel Plant Homeo Domain Protein, Participates in Regulating Cellulase Gene Expression in the Filamentous Fungus Trichoderma reesei
title_sort clp1, a novel plant homeo domain protein, participates in regulating cellulase gene expression in the filamentous fungus trichoderma reesei
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6691364/
https://www.ncbi.nlm.nih.gov/pubmed/31447796
http://dx.doi.org/10.3389/fmicb.2019.01700
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