Characterization and disruption of a gene in the maize pathogen Cochliobolus carbonum encoding a cellulase lacking a cellulose binding domain and hinge region.
Identifieur interne : 000C71 ( Main/Exploration ); précédent : 000C70; suivant : 000C72Characterization and disruption of a gene in the maize pathogen Cochliobolus carbonum encoding a cellulase lacking a cellulose binding domain and hinge region.
Auteurs : P. Sposato [États-Unis] ; J H Ahn ; J D WaltonSource :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ]
Descripteurs français
- KwdFr :
- ADN fongique (génétique), Ascomycota (enzymologie), Ascomycota (génétique), Cartographie de restriction (MeSH), Cellulase (composition chimique), Cellulase (génétique), Données de séquences moléculaires (MeSH), Gènes fongiques (MeSH), Mutation (MeSH), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Transformation génétique (MeSH), Zea mays (microbiologie).
- MESH :
- composition chimique : Cellulase.
- enzymologie : Ascomycota.
- génétique : ADN fongique, Ascomycota, Cellulase.
- microbiologie : Zea mays.
- Cartographie de restriction, Données de séquences moléculaires, Gènes fongiques, Mutation, Similitude de séquences d'acides aminés, Sites de fixation, Séquence d'acides aminés, Séquence nucléotidique, Transformation génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Ascomycota (enzymology), Ascomycota (genetics), Base Sequence (MeSH), Binding Sites (MeSH), Cellulase (chemistry), Cellulase (genetics), DNA, Fungal (genetics), Genes, Fungal (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Restriction Mapping (MeSH), Sequence Homology, Amino Acid (MeSH), Transformation, Genetic (MeSH), Zea mays (microbiology).
- MESH :
- chemical , chemistry : Cellulase.
- enzymology : Ascomycota.
- genetics : Ascomycota, Cellulase, DNA, Fungal.
- microbiology : Zea mays.
- Amino Acid Sequence, Base Sequence, Binding Sites, Genes, Fungal, Molecular Sequence Data, Mutation, Restriction Mapping, Sequence Homology, Amino Acid, Transformation, Genetic.
Abstract
A gene, CEL1, in the maize pathogen Cochliobolus carbonum was identified using the cbh1-3 gene of Phanerochaete chrysosporium as a heterologous probe. The predicted product of CEL1, Cel1, is 62% identical and 71% similar to the product of cbh1-3 and 54 to 62% identical to five cellobiohydrolases from other filamentous fungi. The location of the polyadenylation site 221 bp downstream of the stop codon and the location of a single intron of 55 bp were identified by comparison of the sequences of genomic and cDNA copies of CEL1. The transcriptional start site was determined by rapid amplification of cDNA ends (RACE) to be 39 bp upstream of the putative translational start site. CEL1 mRNA abundance is high when C. carbonum is grown on cellulose or maize cell walls but is undetectable when grown on 2% sucrose or cellulose plus sucrose. Cel1 has a predicted signal peptide of 18 amino acids and therefore a mature size of 46.4 kDa. Like the product of cbh1-1 of P. chrysosporium, but unlike most other endoglucanases and cellobiohydrolases (including the predicted product of cbh1-3), Cel1 does not have a putative cellulose binding domain or associated hinge region. The codon bias of CEL1 is stronger than the bias of cbh1-1 and comparable to that of cbh1-3 and that of the C. carbonum genes PGN1 and XYL1, (encoding endopolygalacturonase and endo-xylanase, respectively). A strain of C. carbonum specifically mutated at CEL1 was produced by transformation with a truncated copy of CEL1. Integration and disruption of CEL1 in the mutant was confirmed by DNA and RNA blotting. Pathogenicity of the CEL1 mutant was indistinguishable from the wild-type, indicating that CEL1 by itself is not a critical disease determinant. Culture filtrates of C. carbonum grown on cellulose or maize cell walls had several cellobiohydrolase, endoglucanase, and beta-glucosidase activities that were separable by chromatofocusing, hydrophobic interaction, or ion-exchange high-performance liquid chromatography.(ABSTRACT TRUNCATED AT 250 WORDS)
DOI: 10.1094/mpmi-8-0602
PubMed: 8589415
Affiliations:
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Sposato</name><affiliation wicri:level="4"><nlm:affiliation>DOE-Plant Research Laboratory, Michigan State University, E. Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>DOE-Plant Research Laboratory, Michigan State University, E. Lansing 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Ahn, J H" sort="Ahn, J H" uniqKey="Ahn J" first="J H" last="Ahn">J H Ahn</name></author><author><name sortKey="Walton, J D" sort="Walton, J D" uniqKey="Walton J" first="J D" last="Walton">J D Walton</name></author></analytic><series><title level="j">Molecular plant-microbe interactions : MPMI</title><idno type="ISSN">0894-0282</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Ascomycota (enzymology)</term><term>Ascomycota (genetics)</term><term>Base Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Cellulase (chemistry)</term><term>Cellulase (genetics)</term><term>DNA, Fungal (genetics)</term><term>Genes, Fungal (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutation (MeSH)</term><term>Restriction Mapping (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Transformation, Genetic (MeSH)</term><term>Zea mays (microbiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN fongique (génétique)</term><term>Ascomycota (enzymologie)</term><term>Ascomycota (génétique)</term><term>Cartographie de restriction (MeSH)</term><term>Cellulase (composition chimique)</term><term>Cellulase (génétique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Gènes fongiques (MeSH)</term><term>Mutation (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Transformation génétique (MeSH)</term><term>Zea mays (microbiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Ascomycota</term><term>Cellulase</term><term>DNA, Fungal</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN fongique</term><term>Ascomycota</term><term>Cellulase</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Zea mays</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Zea mays</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Binding Sites</term><term>Genes, Fungal</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Restriction Mapping</term><term>Sequence Homology, Amino Acid</term><term>Transformation, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cartographie de restriction</term><term>Données de séquences moléculaires</term><term>Gènes fongiques</term><term>Mutation</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Transformation génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A gene, CEL1, in the maize pathogen Cochliobolus carbonum was identified using the cbh1-3 gene of Phanerochaete chrysosporium as a heterologous probe. The predicted product of CEL1, Cel1, is 62% identical and 71% similar to the product of cbh1-3 and 54 to 62% identical to five cellobiohydrolases from other filamentous fungi. The location of the polyadenylation site 221 bp downstream of the stop codon and the location of a single intron of 55 bp were identified by comparison of the sequences of genomic and cDNA copies of CEL1. The transcriptional start site was determined by rapid amplification of cDNA ends (RACE) to be 39 bp upstream of the putative translational start site. CEL1 mRNA abundance is high when C. carbonum is grown on cellulose or maize cell walls but is undetectable when grown on 2% sucrose or cellulose plus sucrose. Cel1 has a predicted signal peptide of 18 amino acids and therefore a mature size of 46.4 kDa. Like the product of cbh1-1 of P. chrysosporium, but unlike most other endoglucanases and cellobiohydrolases (including the predicted product of cbh1-3), Cel1 does not have a putative cellulose binding domain or associated hinge region. The codon bias of CEL1 is stronger than the bias of cbh1-1 and comparable to that of cbh1-3 and that of the C. carbonum genes PGN1 and XYL1, (encoding endopolygalacturonase and endo-xylanase, respectively). A strain of C. carbonum specifically mutated at CEL1 was produced by transformation with a truncated copy of CEL1. Integration and disruption of CEL1 in the mutant was confirmed by DNA and RNA blotting. Pathogenicity of the CEL1 mutant was indistinguishable from the wild-type, indicating that CEL1 by itself is not a critical disease determinant. Culture filtrates of C. carbonum grown on cellulose or maize cell walls had several cellobiohydrolase, endoglucanase, and beta-glucosidase activities that were separable by chromatofocusing, hydrophobic interaction, or ion-exchange high-performance liquid chromatography.(ABSTRACT TRUNCATED AT 250 WORDS)</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8589415</PMID><DateCompleted><Year>1996</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0894-0282</ISSN><JournalIssue CitedMedium="Print"><Volume>8</Volume><Issue>4</Issue><PubDate><MedlineDate>1995 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Molecular plant-microbe interactions : MPMI</Title><ISOAbbreviation>Mol Plant Microbe Interact</ISOAbbreviation></Journal><ArticleTitle>Characterization and disruption of a gene in the maize pathogen Cochliobolus carbonum encoding a cellulase lacking a cellulose binding domain and hinge region.</ArticleTitle><Pagination><MedlinePgn>602-9</MedlinePgn></Pagination><Abstract><AbstractText>A gene, CEL1, in the maize pathogen Cochliobolus carbonum was identified using the cbh1-3 gene of Phanerochaete chrysosporium as a heterologous probe. The predicted product of CEL1, Cel1, is 62% identical and 71% similar to the product of cbh1-3 and 54 to 62% identical to five cellobiohydrolases from other filamentous fungi. The location of the polyadenylation site 221 bp downstream of the stop codon and the location of a single intron of 55 bp were identified by comparison of the sequences of genomic and cDNA copies of CEL1. The transcriptional start site was determined by rapid amplification of cDNA ends (RACE) to be 39 bp upstream of the putative translational start site. CEL1 mRNA abundance is high when C. carbonum is grown on cellulose or maize cell walls but is undetectable when grown on 2% sucrose or cellulose plus sucrose. Cel1 has a predicted signal peptide of 18 amino acids and therefore a mature size of 46.4 kDa. Like the product of cbh1-1 of P. chrysosporium, but unlike most other endoglucanases and cellobiohydrolases (including the predicted product of cbh1-3), Cel1 does not have a putative cellulose binding domain or associated hinge region. The codon bias of CEL1 is stronger than the bias of cbh1-1 and comparable to that of cbh1-3 and that of the C. carbonum genes PGN1 and XYL1, (encoding endopolygalacturonase and endo-xylanase, respectively). A strain of C. carbonum specifically mutated at CEL1 was produced by transformation with a truncated copy of CEL1. Integration and disruption of CEL1 in the mutant was confirmed by DNA and RNA blotting. Pathogenicity of the CEL1 mutant was indistinguishable from the wild-type, indicating that CEL1 by itself is not a critical disease determinant. Culture filtrates of C. carbonum grown on cellulose or maize cell walls had several cellobiohydrolase, endoglucanase, and beta-glucosidase activities that were separable by chromatofocusing, hydrophobic interaction, or ion-exchange high-performance liquid chromatography.(ABSTRACT TRUNCATED AT 250 WORDS)</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sposato</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>DOE-Plant Research Laboratory, Michigan State University, E. Lansing 48824, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahn</LastName><ForeName>J H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Walton</LastName><ForeName>J D</ForeName><Initials>JD</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>U25129</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Plant Microbe Interact</MedlineTA><NlmUniqueID>9107902</NlmUniqueID><ISSNLinking>0894-0282</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>CEL1</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001203" MajorTopicYN="N">Ascomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="Y">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015183" MajorTopicYN="N">Restriction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014170" MajorTopicYN="N">Transformation, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003313" MajorTopicYN="N">Zea mays</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>7</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8589415</ArticleId><ArticleId IdType="doi">10.1094/mpmi-8-0602</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Ahn, J H" sort="Ahn, J H" uniqKey="Ahn J" first="J H" last="Ahn">J H Ahn</name><name sortKey="Walton, J D" sort="Walton, J D" uniqKey="Walton J" first="J D" last="Walton">J D Walton</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Sposato, P" sort="Sposato, P" uniqKey="Sposato P" first="P" last="Sposato">P. 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