Differential regulation of Pleurotus ostreatus dye peroxidases gene expression in response to dyes and potential application of recombinant Pleos-DyP1 in decolorization.
Identifieur interne : 000298 ( Main/Exploration ); précédent : 000297; suivant : 000299Differential regulation of Pleurotus ostreatus dye peroxidases gene expression in response to dyes and potential application of recombinant Pleos-DyP1 in decolorization.
Auteurs : J. Cuamatzi-Flores [Mexique] ; E. Esquivel-Naranjo [Mexique] ; S. Nava-Galicia [Mexique] ; A. L Pez-Munguía [Mexique] ; A. Arroyo-Becerra [Mexique] ; M A Villalobos-L Pez [Mexique] ; M. Bibbins-Martínez [Mexique]Source :
- PloS one [ 1932-6203 ] ; 2019.
Descripteurs français
- KwdFr :
- Acides sulfoniques (MeSH), Agents colorants (composition chimique), Agents colorants (métabolisme), Anthraquinones (MeSH), Composés azoïques (MeSH), Couleur (MeSH), Dépollution biologique de l'environnement (MeSH), Expression des gènes (génétique), Myeloperoxidase (métabolisme), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Peroxidases (génétique), Peroxidases (métabolisme), Pleurotus (génétique), Pleurotus (métabolisme), Régulation de l'expression des gènes (génétique), Salicylates (MeSH).
- MESH :
- composition chimique : Agents colorants.
- génétique : Expression des gènes, Peroxidases, Pleurotus, Régulation de l'expression des gènes.
- métabolisme : Agents colorants, Myeloperoxidase, Oxidoreductases, Peroxidases, Pleurotus.
- Acides sulfoniques, Anthraquinones, Composés azoïques, Couleur, Dépollution biologique de l'environnement, Oxydoréduction, Salicylates.
English descriptors
- KwdEn :
- Anthraquinones (MeSH), Azo Compounds (MeSH), Biodegradation, Environmental (MeSH), Color (MeSH), Coloring Agents (chemistry), Coloring Agents (metabolism), Gene Expression (genetics), Gene Expression Regulation (genetics), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Peroxidase (metabolism), Peroxidases (genetics), Peroxidases (metabolism), Pleurotus (genetics), Pleurotus (metabolism), Salicylates (MeSH), Sulfonic Acids (MeSH).
- MESH :
- chemical , chemistry : Coloring Agents.
- chemical , genetics : Peroxidases.
- chemical , metabolism : Coloring Agents, Oxidoreductases, Peroxidase, Peroxidases.
- chemical : Anthraquinones, Azo Compounds, Salicylates, Sulfonic Acids.
- genetics : Gene Expression, Gene Expression Regulation, Pleurotus.
- metabolism : Pleurotus.
- Biodegradation, Environmental, Color, Oxidation-Reduction.
Abstract
Dye-decolorizing peroxidase (DyP) from the white rot basidiomycete Pleurotus ostreatus is a heme peroxidase able to oxidize diverse substrates, including recalcitrant phenols and dyes. This study analyzed the effect of chemical dyes on P. ostreatus growth, DyP activity and the expression of four Pleos-dyp genes during the time-course of Pleurotus ostreatus cultures containing either Acetyl Yellow G (AYG), Remazol Brilliant Blue R (RBBR) or Acid Blue 129 (AB129) dyes. Additionally, Pleos DyP1 was heterologously expressed in the filamentous fungus Trichoderma atroviride in order to explore the potential of a secreted recombinant enzyme for decolorizing different dyes in cultures and plate assays. The addition of dyes had an induction effect on the enzymatic activity, with the fermentations undertaken using RBBR and AYG dyes presenting the highest total DyP activity. DyP gene expression profiles displayed up/down regulation during the culture of three Pleos-dyp genes (Pleos-dyp1, Pleos-dyp2 and Pleos-dyp4), while Pleos-dyp3 transcript was not detected under any of the culture conditions studied. A 14-fold relative induction level (log2) increase for Pleos-dyp2 and Pleos-dyp4 in AB129 and AYG, respectively, was also found. The presence of AB129 resulted in the highest Pleos-dyp1 gene induction and repression level, corresponding to 11.83 and -14.6-fold relative expression and repression levels, respectively. The lowest expression level of all genes was observed in RBBR, a response which is associated with the growth phase. The filamentous fungus Trichoderma atroviride was successfully transformed for the heterologous expression of Pleos-dyp1. The modified strains (TaDyP) were able to decolorize mono-azo, di-azo, anthraquinone and anthracenedione dyes with extracellular DyP1 activity found in the culture supernatant. After 96 h of culture, the recombinant TaDyP strains were able to degrade (decolorize) 77 and 34% of 0.05mM AB129 and 0.25mM AYG, respectively.
DOI: 10.1371/journal.pone.0209711
PubMed: 30608975
PubMed Central: PMC6319807
Affiliations:
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Esquivel-Naranjo</name><affiliation wicri:level="1"><nlm:affiliation>Facultad de Ciencias Naturales, Universidad Autónoma de Querétaro, Avenida de las Ciencias S/N Juriquilla, Querétaro, México.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Mexique</country><wicri:regionArea>Facultad de Ciencias Naturales, Universidad Autónoma de Querétaro, Avenida de las Ciencias S/N Juriquilla, Querétaro</wicri:regionArea><wicri:noRegion>Querétaro</wicri:noRegion></affiliation></author><author><name sortKey="Nava Galicia, S" sort="Nava Galicia, S" uniqKey="Nava Galicia S" first="S" last="Nava-Galicia">S. Nava-Galicia</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Mexique</country><wicri:regionArea>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala</wicri:regionArea><wicri:noRegion>Tlaxcala</wicri:noRegion></affiliation></author><author><name sortKey="L Pez Munguia, A" sort="L Pez Munguia, A" uniqKey="L Pez Munguia A" first="A" last="L Pez-Munguía">A. L Pez-Munguía</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Biotecnología, Universidad Autónoma de México, Av. Universidad, Chamilpa, Cuernavaca, Morelos, México.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Mexique</country><wicri:regionArea>Instituto de Biotecnología, Universidad Autónoma de México, Av. Universidad, Chamilpa, Cuernavaca, Morelos</wicri:regionArea><wicri:noRegion>Morelos</wicri:noRegion></affiliation></author><author><name sortKey="Arroyo Becerra, A" sort="Arroyo Becerra, A" uniqKey="Arroyo Becerra A" first="A" last="Arroyo-Becerra">A. Arroyo-Becerra</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Mexique</country><wicri:regionArea>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala</wicri:regionArea><wicri:noRegion>Tlaxcala</wicri:noRegion></affiliation></author><author><name sortKey="Villalobos L Pez, M A" sort="Villalobos L Pez, M A" uniqKey="Villalobos L Pez M" first="M A" last="Villalobos-L Pez">M A Villalobos-L Pez</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Mexique</country><wicri:regionArea>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala</wicri:regionArea><wicri:noRegion>Tlaxcala</wicri:noRegion></affiliation></author><author><name sortKey="Bibbins Martinez, M" sort="Bibbins Martinez, M" uniqKey="Bibbins Martinez M" first="M" last="Bibbins-Martínez">M. Bibbins-Martínez</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Mexique</country><wicri:regionArea>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala</wicri:regionArea><wicri:noRegion>Tlaxcala</wicri:noRegion></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anthraquinones (MeSH)</term><term>Azo Compounds (MeSH)</term><term>Biodegradation, Environmental (MeSH)</term><term>Color (MeSH)</term><term>Coloring Agents (chemistry)</term><term>Coloring Agents (metabolism)</term><term>Gene Expression (genetics)</term><term>Gene Expression Regulation (genetics)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidase (metabolism)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Pleurotus (genetics)</term><term>Pleurotus (metabolism)</term><term>Salicylates (MeSH)</term><term>Sulfonic Acids (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides sulfoniques (MeSH)</term><term>Agents colorants (composition chimique)</term><term>Agents colorants (métabolisme)</term><term>Anthraquinones (MeSH)</term><term>Composés azoïques (MeSH)</term><term>Couleur (MeSH)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Expression des gènes (génétique)</term><term>Myeloperoxidase (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Pleurotus (génétique)</term><term>Pleurotus (métabolisme)</term><term>Régulation de l'expression des gènes (génétique)</term><term>Salicylates (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Coloring Agents</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Coloring Agents</term><term>Oxidoreductases</term><term>Peroxidase</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Anthraquinones</term><term>Azo Compounds</term><term>Salicylates</term><term>Sulfonic Acids</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Agents colorants</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Gene Expression</term><term>Gene Expression Regulation</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Expression des gènes</term><term>Peroxidases</term><term>Pleurotus</term><term>Régulation de l'expression des gènes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Agents colorants</term><term>Myeloperoxidase</term><term>Oxidoreductases</term><term>Peroxidases</term><term>Pleurotus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Color</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acides sulfoniques</term><term>Anthraquinones</term><term>Composés azoïques</term><term>Couleur</term><term>Dépollution biologique de l'environnement</term><term>Oxydoréduction</term><term>Salicylates</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Dye-decolorizing peroxidase (DyP) from the white rot basidiomycete Pleurotus ostreatus is a heme peroxidase able to oxidize diverse substrates, including recalcitrant phenols and dyes. This study analyzed the effect of chemical dyes on P. ostreatus growth, DyP activity and the expression of four Pleos-dyp genes during the time-course of Pleurotus ostreatus cultures containing either Acetyl Yellow G (AYG), Remazol Brilliant Blue R (RBBR) or Acid Blue 129 (AB129) dyes. Additionally, Pleos DyP1 was heterologously expressed in the filamentous fungus Trichoderma atroviride in order to explore the potential of a secreted recombinant enzyme for decolorizing different dyes in cultures and plate assays. The addition of dyes had an induction effect on the enzymatic activity, with the fermentations undertaken using RBBR and AYG dyes presenting the highest total DyP activity. DyP gene expression profiles displayed up/down regulation during the culture of three Pleos-dyp genes (Pleos-dyp1, Pleos-dyp2 and Pleos-dyp4), while Pleos-dyp3 transcript was not detected under any of the culture conditions studied. A 14-fold relative induction level (log2) increase for Pleos-dyp2 and Pleos-dyp4 in AB129 and AYG, respectively, was also found. The presence of AB129 resulted in the highest Pleos-dyp1 gene induction and repression level, corresponding to 11.83 and -14.6-fold relative expression and repression levels, respectively. The lowest expression level of all genes was observed in RBBR, a response which is associated with the growth phase. The filamentous fungus Trichoderma atroviride was successfully transformed for the heterologous expression of Pleos-dyp1. The modified strains (TaDyP) were able to decolorize mono-azo, di-azo, anthraquinone and anthracenedione dyes with extracellular DyP1 activity found in the culture supernatant. After 96 h of culture, the recombinant TaDyP strains were able to degrade (decolorize) 77 and 34% of 0.05mM AB129 and 0.25mM AYG, respectively.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30608975</PMID><DateCompleted><Year>2019</Year><Month>11</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>14</Volume><Issue>1</Issue><PubDate><Year>2019</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Differential regulation of Pleurotus ostreatus dye peroxidases gene expression in response to dyes and potential application of recombinant Pleos-DyP1 in decolorization.</ArticleTitle><Pagination><MedlinePgn>e0209711</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0209711</ELocationID><Abstract><AbstractText>Dye-decolorizing peroxidase (DyP) from the white rot basidiomycete Pleurotus ostreatus is a heme peroxidase able to oxidize diverse substrates, including recalcitrant phenols and dyes. This study analyzed the effect of chemical dyes on P. ostreatus growth, DyP activity and the expression of four Pleos-dyp genes during the time-course of Pleurotus ostreatus cultures containing either Acetyl Yellow G (AYG), Remazol Brilliant Blue R (RBBR) or Acid Blue 129 (AB129) dyes. Additionally, Pleos DyP1 was heterologously expressed in the filamentous fungus Trichoderma atroviride in order to explore the potential of a secreted recombinant enzyme for decolorizing different dyes in cultures and plate assays. The addition of dyes had an induction effect on the enzymatic activity, with the fermentations undertaken using RBBR and AYG dyes presenting the highest total DyP activity. DyP gene expression profiles displayed up/down regulation during the culture of three Pleos-dyp genes (Pleos-dyp1, Pleos-dyp2 and Pleos-dyp4), while Pleos-dyp3 transcript was not detected under any of the culture conditions studied. A 14-fold relative induction level (log2) increase for Pleos-dyp2 and Pleos-dyp4 in AB129 and AYG, respectively, was also found. The presence of AB129 resulted in the highest Pleos-dyp1 gene induction and repression level, corresponding to 11.83 and -14.6-fold relative expression and repression levels, respectively. The lowest expression level of all genes was observed in RBBR, a response which is associated with the growth phase. The filamentous fungus Trichoderma atroviride was successfully transformed for the heterologous expression of Pleos-dyp1. The modified strains (TaDyP) were able to decolorize mono-azo, di-azo, anthraquinone and anthracenedione dyes with extracellular DyP1 activity found in the culture supernatant. After 96 h of culture, the recombinant TaDyP strains were able to degrade (decolorize) 77 and 34% of 0.05mM AB129 and 0.25mM AYG, respectively.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cuamatzi-Flores</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Esquivel-Naranjo</LastName><ForeName>E</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Facultad de Ciencias Naturales, Universidad Autónoma de Querétaro, Avenida de las Ciencias S/N Juriquilla, Querétaro, México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nava-Galicia</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>López-Munguía</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Instituto de Biotecnología, Universidad Autónoma de México, Av. Universidad, Chamilpa, Cuernavaca, Morelos, México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Arroyo-Becerra</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Villalobos-López</LastName><ForeName>M A</ForeName><Initials>MA</Initials><Identifier Source="ORCID">0000-0002-8640-342X</Identifier><AffiliationInfo><Affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bibbins-Martínez</LastName><ForeName>M</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0001-9980-5041</Identifier><AffiliationInfo><Affiliation>Centro de Investigación en Biotecnología Aplicada-Instituto Politécnico Nacional, Ex-Hacienda de San Juan Molino, Tepetitla de Lardizábal, Tlaxcala, México.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>01</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C532474">1-amino-4-(2,4,6-trimethylanilino)anthraquinone-2-sulfonate</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000880">Anthraquinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001391">Azo Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004396">Coloring Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012459">Salicylates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013451">Sulfonic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C554668">alizarin yellow GG</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>L51IMM9UP9</RegistryNumber><NameOfSubstance UI="C024758">Remazol Brilliant Blue R</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>PLoS One. 2019 Mar 7;14(3):e0213798</RefSource><PMID Version="1">30845247</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000880" MajorTopicYN="N">Anthraquinones</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001391" MajorTopicYN="N">Azo Compounds</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003116" MajorTopicYN="N">Color</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" MajorTopicYN="N">Pleurotus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012459" MajorTopicYN="N">Salicylates</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013451" MajorTopicYN="N">Sulfonic Acids</DescriptorName></MeshHeading></MeshHeadingList><CoiStatement>The authors have declared that no competing interest exist.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate 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