Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium.
Identifieur interne : 000C64 ( Main/Exploration ); précédent : 000C63; suivant : 000C65Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium.
Auteurs : B. Li [États-Unis] ; S R Nagalla ; V. RenganathanSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1996.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ADN fongique (génétique), Amorces ADN (génétique), Basidiomycota (enzymologie), Basidiomycota (génétique), Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (génétique), Cellulose (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Réaction de polymérisation en chaîne (MeSH), Similitude de séquences d'acides aminés (MeSH), Similitude de séquences d'acides nucléiques (MeSH), Sites de fixation (MeSH), Structure moléculaire (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Carbohydrate dehydrogenases.
- enzymologie : Basidiomycota.
- génétique : ADN complémentaire, ADN fongique, Amorces ADN, Basidiomycota, Carbohydrate dehydrogenases.
- Cellulose, Clonage moléculaire, Données de séquences moléculaires, Réaction de polymérisation en chaîne, Similitude de séquences d'acides aminés, Similitude de séquences d'acides nucléiques, Sites de fixation, Structure moléculaire, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Basidiomycota (enzymology), Basidiomycota (genetics), Binding Sites (MeSH), Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (genetics), Cellulose (MeSH), Cloning, Molecular (MeSH), DNA Primers (genetics), DNA, Complementary (genetics), DNA, Fungal (genetics), Molecular Sequence Data (MeSH), Molecular Structure (MeSH), Polymerase Chain Reaction (MeSH), Sequence Homology, Amino Acid (MeSH), Sequence Homology, Nucleic Acid (MeSH).
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases.
- enzymology : Basidiomycota.
- genetics : Basidiomycota, Carbohydrate Dehydrogenases, DNA Primers, DNA, Complementary, DNA, Fungal.
- Amino Acid Sequence, Base Sequence, Binding Sites, Cellulose, Cloning, Molecular, Molecular Sequence Data, Molecular Structure, Polymerase Chain Reaction, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid.
Abstract
Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of the wood-degrading basidiomycete Phanerochaete chrysosporium. CDH contains one flavin adenine dinucleotide (FAD) and one heme b per molecule, and it oxidizes cellobiose to cellobionolactone. In this report, a 2.4-kb cDNA encoding CDH was isolated by screening an expression library of P. chrysosporium OGC101 with a CDH-specific polyclonal antibody. The cDNA encodes a 755-amino-acid protein with a predicted mass of 80,115 Da. Sequence analysis suggests that the heme domain is located at the N terminus and that the falvin domain is located at the C terminus. The flavin domain shows a beta 1-alpha A-beta 2 motif for FAD binding and has high sequence similarity to several FAD-dependent enzymes. Little sequence similarity to hemoflavoenzymes is found. CDH binds to cellulose similarly to cellulases. However, little sequence similarity is observed with the conserved cellulose-binding sequences of cellulases. This suggests that CDH might possess a specific sequence for cellulose binding which is different from that of cellulases. Northern (RNA) blot analysis of total RNA from cellulose-, glucose-, and cellobiose-grown P. chrysosporium indicated that CDH mRNA is produced only in cellulose-grown cells. This suggests that CDH expression is regulated at the transcriptional level by either cellulose or one of its degradation products. Southern blot analysis suggests the presence of only a single gene for CDH in P. chrysosporium OGC101.
DOI: 10.1128/AEM.62.4.1329-1335.1996
PubMed: 8919793
PubMed Central: PMC167898
Affiliations:
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Li</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000</wicri:regionArea><placeName><settlement type="city">Portland</settlement><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Nagalla, S R" sort="Nagalla, S R" uniqKey="Nagalla S" first="S R" last="Nagalla">S R Nagalla</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="ISSN">0099-2240</idno><imprint><date when="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Basidiomycota (genetics)</term><term>Binding Sites (MeSH)</term><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Carbohydrate Dehydrogenases (genetics)</term><term>Cellulose (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA Primers (genetics)</term><term>DNA, Complementary (genetics)</term><term>DNA, Fungal (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Structure (MeSH)</term><term>Polymerase Chain Reaction (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Sequence Homology, Nucleic Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>ADN fongique (génétique)</term><term>Amorces ADN (génétique)</term><term>Basidiomycota (enzymologie)</term><term>Basidiomycota (génétique)</term><term>Carbohydrate dehydrogenases (composition chimique)</term><term>Carbohydrate dehydrogenases (génétique)</term><term>Cellulose (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Réaction de polymérisation en chaîne (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Similitude de séquences d'acides nucléiques (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Structure moléculaire (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carbohydrate dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Basidiomycota</term><term>Carbohydrate Dehydrogenases</term><term>DNA Primers</term><term>DNA, Complementary</term><term>DNA, Fungal</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>ADN fongique</term><term>Amorces ADN</term><term>Basidiomycota</term><term>Carbohydrate dehydrogenases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Binding Sites</term><term>Cellulose</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term><term>Molecular Structure</term><term>Polymerase Chain Reaction</term><term>Sequence Homology, Amino Acid</term><term>Sequence Homology, Nucleic Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellulose</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Réaction de polymérisation en chaîne</term><term>Similitude de séquences d'acides aminés</term><term>Similitude de séquences d'acides nucléiques</term><term>Sites de fixation</term><term>Structure moléculaire</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of the wood-degrading basidiomycete Phanerochaete chrysosporium. CDH contains one flavin adenine dinucleotide (FAD) and one heme b per molecule, and it oxidizes cellobiose to cellobionolactone. In this report, a 2.4-kb cDNA encoding CDH was isolated by screening an expression library of P. chrysosporium OGC101 with a CDH-specific polyclonal antibody. The cDNA encodes a 755-amino-acid protein with a predicted mass of 80,115 Da. Sequence analysis suggests that the heme domain is located at the N terminus and that the falvin domain is located at the C terminus. The flavin domain shows a beta 1-alpha A-beta 2 motif for FAD binding and has high sequence similarity to several FAD-dependent enzymes. Little sequence similarity to hemoflavoenzymes is found. CDH binds to cellulose similarly to cellulases. However, little sequence similarity is observed with the conserved cellulose-binding sequences of cellulases. This suggests that CDH might possess a specific sequence for cellulose binding which is different from that of cellulases. Northern (RNA) blot analysis of total RNA from cellulose-, glucose-, and cellobiose-grown P. chrysosporium indicated that CDH mRNA is produced only in cellulose-grown cells. This suggests that CDH expression is regulated at the transcriptional level by either cellulose or one of its degradation products. Southern blot analysis suggests the presence of only a single gene for CDH in P. chrysosporium OGC101.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8919793</PMID><DateCompleted><Year>1997</Year><Month>01</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>62</Volume><Issue>4</Issue><PubDate><Year>1996</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>1329-35</MedlinePgn></Pagination><Abstract><AbstractText>Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of the wood-degrading basidiomycete Phanerochaete chrysosporium. CDH contains one flavin adenine dinucleotide (FAD) and one heme b per molecule, and it oxidizes cellobiose to cellobionolactone. In this report, a 2.4-kb cDNA encoding CDH was isolated by screening an expression library of P. chrysosporium OGC101 with a CDH-specific polyclonal antibody. The cDNA encodes a 755-amino-acid protein with a predicted mass of 80,115 Da. Sequence analysis suggests that the heme domain is located at the N terminus and that the falvin domain is located at the C terminus. The flavin domain shows a beta 1-alpha A-beta 2 motif for FAD binding and has high sequence similarity to several FAD-dependent enzymes. Little sequence similarity to hemoflavoenzymes is found. CDH binds to cellulose similarly to cellulases. However, little sequence similarity is observed with the conserved cellulose-binding sequences of cellulases. This suggests that CDH might possess a specific sequence for cellulose binding which is different from that of cellulases. Northern (RNA) blot analysis of total RNA from cellulose-, glucose-, and cellobiose-grown P. chrysosporium indicated that CDH mRNA is produced only in cellulose-grown cells. This suggests that CDH expression is regulated at the transcriptional level by either cellulose or one of its degradation products. Southern blot analysis suggests the presence of only a single gene for CDH in P. chrysosporium OGC101.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nagalla</LastName><ForeName>S R</ForeName><Initials>SR</Initials></Author><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>U46081</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Environ Microbiol</MedlineTA><NlmUniqueID>7605801</NlmUniqueID><ISSNLinking>0099-2240</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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Nagalla</name><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></noCountry><country name="États-Unis"><region name="Oregon"><name sortKey="Li, B" sort="Li, B" uniqKey="Li B" first="B" last="Li">B. Li</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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