The Nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol
The nag1 gene of the mycoparasitic fungus Trichoderma atroviride encodes a 73-kDa N-acetyl-beta- d-glucosaminidase, which is secreted into the medium and partially bound to the cell wall. To elucidate the role of this enzyme in chitinase induction and biocontrol, a nag1-disruption mutant was prepare...
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Veröffentlicht in: | Current genetics 2003-07, Vol.43 (4), p.289-295 |
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description | The nag1 gene of the mycoparasitic fungus Trichoderma atroviride encodes a 73-kDa N-acetyl-beta- d-glucosaminidase, which is secreted into the medium and partially bound to the cell wall. To elucidate the role of this enzyme in chitinase induction and biocontrol, a nag1-disruption mutant was prepared. It displayed only 4% of the original N-acetyl-beta- d-glucosaminidase activity, indicating that the nag1 gene product accounts for the majority of this activity in T. atroviride. The nag1-disruption strain was indistinguishable from the parent strain in growth and morphology, but exhibited delayed autolysis. Northern analysis showed that colloidal chitin disruption does not induce ech42 gene transcription in the nag1-disruption strain. Enzyme activities capable of hydrolysing p-nitrophenyl- N, N'-diacetylchitobioside and p-nitrophenyl- N, N'-diacetylchitotriose were also absent from the nag1-disruption strain under the same conditions. Retransformation of the T. atroviride nag1-disruption strain with the nag1 gene essentially led to the parent-type behaviour in all these experiments. However, addition of N-acetyl-beta- d-glucosaminidase to the medium of the nag1-disruption strain did not rescue the mutant phenotype. The disruption- nag1 strain showed 30% reduced ability to protect beans against infection by Rhizoctonia solani and Sclerotinia sclerotiorum. The data indicate that nag1 is essential for triggering chitinase gene expression in T. atroviride and that its functional impairment reduces biocontrol by T. atroviride by a significant extent. |
doi_str_mv | 10.1007/s00294-003-0399-y |
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To elucidate the role of this enzyme in chitinase induction and biocontrol, a nag1-disruption mutant was prepared. It displayed only 4% of the original N-acetyl-beta- d-glucosaminidase activity, indicating that the nag1 gene product accounts for the majority of this activity in T. atroviride. The nag1-disruption strain was indistinguishable from the parent strain in growth and morphology, but exhibited delayed autolysis. Northern analysis showed that colloidal chitin disruption does not induce ech42 gene transcription in the nag1-disruption strain. Enzyme activities capable of hydrolysing p-nitrophenyl- N, N'-diacetylchitobioside and p-nitrophenyl- N, N'-diacetylchitotriose were also absent from the nag1-disruption strain under the same conditions. Retransformation of the T. atroviride nag1-disruption strain with the nag1 gene essentially led to the parent-type behaviour in all these experiments. However, addition of N-acetyl-beta- d-glucosaminidase to the medium of the nag1-disruption strain did not rescue the mutant phenotype. The disruption- nag1 strain showed 30% reduced ability to protect beans against infection by Rhizoctonia solani and Sclerotinia sclerotiorum. The data indicate that nag1 is essential for triggering chitinase gene expression in T. atroviride and that its functional impairment reduces biocontrol by T. atroviride by a significant extent.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/s00294-003-0399-y</identifier><identifier>PMID: 12748812</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Acetylglucosaminidase - chemistry ; Acetylglucosaminidase - physiology ; Biological control ; Blotting, Northern ; Chitin ; Chitin - chemistry ; Chitinase ; Chitinases - metabolism ; DNA - metabolism ; Enzymatic activity ; Enzyme-Linked Immunosorbent Assay ; Gene Deletion ; Gene expression ; Models, Genetic ; Mutation ; Phenotype ; Plasmids - metabolism ; Proteins ; RNA - metabolism ; Trichoderma - enzymology</subject><ispartof>Current genetics, 2003-07, Vol.43 (4), p.289-295</ispartof><rights>Springer-Verlag 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c355t-c9c636cfcea0bb6d12c1dc0d736a0e64e586f1ec68a4d51f807af8cfcf98fedb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12748812$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brunner, Kurt</creatorcontrib><creatorcontrib>Peterbauer, Clemens K</creatorcontrib><creatorcontrib>Mach, Robert L</creatorcontrib><creatorcontrib>Lorito, Matteo</creatorcontrib><creatorcontrib>Zeilinger, Susanne</creatorcontrib><creatorcontrib>Kubicek, Christian P</creatorcontrib><title>The Nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><description>The nag1 gene of the mycoparasitic fungus Trichoderma atroviride encodes a 73-kDa N-acetyl-beta- d-glucosaminidase, which is secreted into the medium and partially bound to the cell wall. To elucidate the role of this enzyme in chitinase induction and biocontrol, a nag1-disruption mutant was prepared. It displayed only 4% of the original N-acetyl-beta- d-glucosaminidase activity, indicating that the nag1 gene product accounts for the majority of this activity in T. atroviride. The nag1-disruption strain was indistinguishable from the parent strain in growth and morphology, but exhibited delayed autolysis. Northern analysis showed that colloidal chitin disruption does not induce ech42 gene transcription in the nag1-disruption strain. Enzyme activities capable of hydrolysing p-nitrophenyl- N, N'-diacetylchitobioside and p-nitrophenyl- N, N'-diacetylchitotriose were also absent from the nag1-disruption strain under the same conditions. Retransformation of the T. atroviride nag1-disruption strain with the nag1 gene essentially led to the parent-type behaviour in all these experiments. However, addition of N-acetyl-beta- d-glucosaminidase to the medium of the nag1-disruption strain did not rescue the mutant phenotype. The disruption- nag1 strain showed 30% reduced ability to protect beans against infection by Rhizoctonia solani and Sclerotinia sclerotiorum. The data indicate that nag1 is essential for triggering chitinase gene expression in T. atroviride and that its functional impairment reduces biocontrol by T. atroviride by a significant extent.</description><subject>Acetylglucosaminidase - chemistry</subject><subject>Acetylglucosaminidase - physiology</subject><subject>Biological control</subject><subject>Blotting, Northern</subject><subject>Chitin</subject><subject>Chitin - chemistry</subject><subject>Chitinase</subject><subject>Chitinases - metabolism</subject><subject>DNA - metabolism</subject><subject>Enzymatic activity</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Gene Deletion</subject><subject>Gene expression</subject><subject>Models, Genetic</subject><subject>Mutation</subject><subject>Phenotype</subject><subject>Plasmids - metabolism</subject><subject>Proteins</subject><subject>RNA - metabolism</subject><subject>Trichoderma - enzymology</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkcuKFDEUhoMoTjv6AG4kuHAXPUnqklrKMF5gGDftOqSSk-k0VcmYVA3US_jMpukGwY2rwOH7_0POR8hbDh85QP-pAIihYQCSgRwGtj0jO95IwWBQ8jnZAe8FU6DkFXlVyhGACzX0L8kVF32jFBc78nt_QHpvHji9Z8bisk0P02pTMXOIwZmCNHm6z8EeksM8G2qWnJ5CDg5pKBRLwbgEM1GfMrWHsIR4CoXoVruEFOm4XcbURHcqm82xohknfDLRIl0SHUOyKdbi6TV54c1U8M3lvSY_v9zub76xux9fv998vmNWtu3C7GA72Vlv0cA4do4Ly50F18vOAHYNtqrzHG2nTONa7hX0xqvK-0F5dKO8Jh_OvY85_VqxLHoOxeI0mYhpLbqXbb0V7_8LcqVANCAq-P4f8JjWHOsndN3eCZBcVYifIZtTKRm9fsxhNnnTHPRJqT4r1VWpPinVW828uxSv44zub-LiUP4B-RKgKw</recordid><startdate>200307</startdate><enddate>200307</enddate><creator>Brunner, Kurt</creator><creator>Peterbauer, Clemens K</creator><creator>Mach, Robert L</creator><creator>Lorito, Matteo</creator><creator>Zeilinger, Susanne</creator><creator>Kubicek, Christian P</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200307</creationdate><title>The Nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol</title><author>Brunner, Kurt ; Peterbauer, Clemens K ; Mach, Robert L ; Lorito, Matteo ; Zeilinger, Susanne ; Kubicek, Christian P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-c9c636cfcea0bb6d12c1dc0d736a0e64e586f1ec68a4d51f807af8cfcf98fedb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetylglucosaminidase - chemistry</topic><topic>Acetylglucosaminidase - physiology</topic><topic>Biological control</topic><topic>Blotting, Northern</topic><topic>Chitin</topic><topic>Chitin - chemistry</topic><topic>Chitinase</topic><topic>Chitinases - metabolism</topic><topic>DNA - metabolism</topic><topic>Enzymatic activity</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Gene Deletion</topic><topic>Gene expression</topic><topic>Models, Genetic</topic><topic>Mutation</topic><topic>Phenotype</topic><topic>Plasmids - metabolism</topic><topic>Proteins</topic><topic>RNA - metabolism</topic><topic>Trichoderma - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brunner, Kurt</creatorcontrib><creatorcontrib>Peterbauer, Clemens K</creatorcontrib><creatorcontrib>Mach, Robert L</creatorcontrib><creatorcontrib>Lorito, Matteo</creatorcontrib><creatorcontrib>Zeilinger, Susanne</creatorcontrib><creatorcontrib>Kubicek, Christian P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Current genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brunner, Kurt</au><au>Peterbauer, Clemens K</au><au>Mach, Robert L</au><au>Lorito, Matteo</au><au>Zeilinger, Susanne</au><au>Kubicek, Christian P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol</atitle><jtitle>Current genetics</jtitle><addtitle>Curr Genet</addtitle><date>2003-07</date><risdate>2003</risdate><volume>43</volume><issue>4</issue><spage>289</spage><epage>295</epage><pages>289-295</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><abstract>The nag1 gene of the mycoparasitic fungus Trichoderma atroviride encodes a 73-kDa N-acetyl-beta- d-glucosaminidase, which is secreted into the medium and partially bound to the cell wall. To elucidate the role of this enzyme in chitinase induction and biocontrol, a nag1-disruption mutant was prepared. It displayed only 4% of the original N-acetyl-beta- d-glucosaminidase activity, indicating that the nag1 gene product accounts for the majority of this activity in T. atroviride. The nag1-disruption strain was indistinguishable from the parent strain in growth and morphology, but exhibited delayed autolysis. Northern analysis showed that colloidal chitin disruption does not induce ech42 gene transcription in the nag1-disruption strain. Enzyme activities capable of hydrolysing p-nitrophenyl- N, N'-diacetylchitobioside and p-nitrophenyl- N, N'-diacetylchitotriose were also absent from the nag1-disruption strain under the same conditions. Retransformation of the T. atroviride nag1-disruption strain with the nag1 gene essentially led to the parent-type behaviour in all these experiments. However, addition of N-acetyl-beta- d-glucosaminidase to the medium of the nag1-disruption strain did not rescue the mutant phenotype. The disruption- nag1 strain showed 30% reduced ability to protect beans against infection by Rhizoctonia solani and Sclerotinia sclerotiorum. The data indicate that nag1 is essential for triggering chitinase gene expression in T. atroviride and that its functional impairment reduces biocontrol by T. atroviride by a significant extent.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>12748812</pmid><doi>10.1007/s00294-003-0399-y</doi><tpages>7</tpages></addata></record> |
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subjects | Acetylglucosaminidase - chemistry Acetylglucosaminidase - physiology Biological control Blotting, Northern Chitin Chitin - chemistry Chitinase Chitinases - metabolism DNA - metabolism Enzymatic activity Enzyme-Linked Immunosorbent Assay Gene Deletion Gene expression Models, Genetic Mutation Phenotype Plasmids - metabolism Proteins RNA - metabolism Trichoderma - enzymology |
title | The Nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol |
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