Molecular cloning and characterization of two intracellular beta-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000769 ( Main/Exploration ); précédent : 000768; suivant : 000770Molecular cloning and characterization of two intracellular beta-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium.
Auteurs : Takeshi Tsukada [Japon] ; Kiyohiko Igarashi ; Makoto Yoshida ; Masahiro SamejimaSource :
- Applied microbiology and biotechnology [ 0175-7598 ] ; 2006.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ADN fongique (composition chimique), ADN fongique (génétique), ARN fongique (biosynthèse), ARN messager (biosynthèse), Analyse de séquence d'ADN (MeSH), Cadres ouverts de lecture (MeSH), Cellobiose (métabolisme), Cinétique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Hétérosides (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines recombinantes (génétique), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), RT-PCR (MeSH), Régulation de l'expression des gènes fongiques (MeSH), Similitude de séquences d'acides aminés (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), bêta-Glucosidase (génétique), bêta-Glucosidase (isolement et purification), bêta-Glucosidase (métabolisme).
- MESH :
- biosynthèse : ARN fongique, ARN messager.
- composition chimique : ADN fongique.
- enzymologie : Phanerochaete.
- génétique : ADN complémentaire, ADN fongique, Phanerochaete, Protéines recombinantes, bêta-Glucosidase.
- isolement et purification : Protéines recombinantes, bêta-Glucosidase.
- métabolisme : Cellobiose, Hétérosides, Protéines recombinantes, bêta-Glucosidase.
- Analyse de séquence d'ADN, Cadres ouverts de lecture, Cinétique, Clonage moléculaire, Données de séquences moléculaires, RT-PCR, Régulation de l'expression des gènes fongiques, Similitude de séquences d'acides aminés, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cellobiose (metabolism), Cloning, Molecular (MeSH), DNA, Complementary (genetics), DNA, Fungal (chemistry), DNA, Fungal (genetics), Gene Expression Regulation, Fungal (MeSH), Glycosides (metabolism), Kinetics (MeSH), Molecular Sequence Data (MeSH), Open Reading Frames (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Protein Structure, Tertiary (MeSH), RNA, Fungal (biosynthesis), RNA, Messenger (biosynthesis), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH), beta-Glucosidase (genetics), beta-Glucosidase (isolation & purification), beta-Glucosidase (metabolism).
- MESH :
- chemical , biosynthesis : RNA, Fungal, RNA, Messenger.
- chemical , chemistry : DNA, Fungal.
- chemical , genetics : DNA, Complementary, DNA, Fungal, Recombinant Proteins, beta-Glucosidase.
- chemical , isolation & purification : Recombinant Proteins, beta-Glucosidase.
- chemical , metabolism : Cellobiose, Glycosides, Recombinant Proteins, beta-Glucosidase.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- Amino Acid Sequence, Cloning, Molecular, Gene Expression Regulation, Fungal, Kinetics, Molecular Sequence Data, Open Reading Frames, Protein Structure, Tertiary, Reverse Transcriptase Polymerase Chain Reaction, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
Abstract
cDNAs encoding two glycoside hydrolase family 1 beta-glucosidases (BGL1A and BGL1B) were cloned from the basidiomycete Phanerochaete chrysosporium, and the substrate specificities of the recombinant enzymes and the expression patterns of the two genes were investigated in relation to cellobiose metabolism by the fungus. The cDNA sequences contained open reading frames of 1,389 base pairs (bp) (bgl1A) and 1,623 bp (bgl1B), encoding 462 and 530 amino acids, respectively. Although high sequence identity (65%) was observed between the deduced amino acid sequences of the two enzymes, an apparent difference was observed at the C-terminal region: BGL1B has a 63-amino acid extension, which has no similarity with any known protein. Both recombinant enzymes expressed in Escherichia coli showed hydrolytic activity towards several beta-glycosidic compounds. However, the substrate recognition patterns of the two enzymes were quite different from each other. In particular, cellobiose was hydrolyzed more effectively by BGL1B than by BGL1A. The expression of the two genes in the fungus was monitored by reverse transcription-PCR, which showed that bgl1A was expressed constitutively in both glucose- and cellobiose-containing culture, whereas bgl1B was expressed in cellobiose culture but was repressed in glucose culture, possibly because of carbon catabolite repression. We conclude that BGL1B contributes to cellobiose metabolism during cellulose degradation by P. chrysosporium.
DOI: 10.1007/s00253-006-0526-z
PubMed: 16896601
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(MeSH)</term><term>Sequence Analysis, DNA (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>beta-Glucosidase (genetics)</term><term>beta-Glucosidase (isolation & purification)</term><term>beta-Glucosidase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>ADN fongique (composition chimique)</term><term>ADN fongique (génétique)</term><term>ARN fongique (biosynthèse)</term><term>ARN messager (biosynthèse)</term><term>Analyse de séquence d'ADN (MeSH)</term><term>Cadres ouverts de lecture (MeSH)</term><term>Cellobiose (métabolisme)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Hétérosides (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (isolement et purification)</term><term>Protéines recombinantes (métabolisme)</term><term>RT-PCR (MeSH)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>bêta-Glucosidase (génétique)</term><term>bêta-Glucosidase (isolement et purification)</term><term>bêta-Glucosidase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>RNA, Fungal</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Fungal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Complementary</term><term>DNA, Fungal</term><term>Recombinant Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellobiose</term><term>Glycosides</term><term>Recombinant Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>ARN fongique</term><term>ARN messager</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>ADN fongique</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>ADN fongique</term><term>Phanerochaete</term><term>Protéines recombinantes</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines recombinantes</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellobiose</term><term>Hétérosides</term><term>Protéines recombinantes</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Gene Expression Regulation, Fungal</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Open Reading Frames</term><term>Protein Structure, Tertiary</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Sequence Analysis, DNA</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Cadres ouverts de lecture</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>RT-PCR</term><term>Régulation de l'expression des gènes fongiques</term><term>Similitude de séquences d'acides aminés</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">cDNAs encoding two glycoside hydrolase family 1 beta-glucosidases (BGL1A and BGL1B) were cloned from the basidiomycete Phanerochaete chrysosporium, and the substrate specificities of the recombinant enzymes and the expression patterns of the two genes were investigated in relation to cellobiose metabolism by the fungus. The cDNA sequences contained open reading frames of 1,389 base pairs (bp) (bgl1A) and 1,623 bp (bgl1B), encoding 462 and 530 amino acids, respectively. Although high sequence identity (65%) was observed between the deduced amino acid sequences of the two enzymes, an apparent difference was observed at the C-terminal region: BGL1B has a 63-amino acid extension, which has no similarity with any known protein. Both recombinant enzymes expressed in Escherichia coli showed hydrolytic activity towards several beta-glycosidic compounds. However, the substrate recognition patterns of the two enzymes were quite different from each other. In particular, cellobiose was hydrolyzed more effectively by BGL1B than by BGL1A. The expression of the two genes in the fungus was monitored by reverse transcription-PCR, which showed that bgl1A was expressed constitutively in both glucose- and cellobiose-containing culture, whereas bgl1B was expressed in cellobiose culture but was repressed in glucose culture, possibly because of carbon catabolite repression. We conclude that BGL1B contributes to cellobiose metabolism during cellulose degradation by P. chrysosporium.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16896601</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>05</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0175-7598</ISSN><JournalIssue CitedMedium="Print"><Volume>73</Volume><Issue>4</Issue><PubDate><Year>2006</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Molecular cloning and characterization of two intracellular beta-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>807-14</MedlinePgn></Pagination><Abstract><AbstractText>cDNAs encoding two glycoside hydrolase family 1 beta-glucosidases (BGL1A and BGL1B) were cloned from the basidiomycete Phanerochaete chrysosporium, and the substrate specificities of the recombinant enzymes and the expression patterns of the two genes were investigated in relation to cellobiose metabolism by the fungus. The cDNA sequences contained open reading frames of 1,389 base pairs (bp) (bgl1A) and 1,623 bp (bgl1B), encoding 462 and 530 amino acids, respectively. Although high sequence identity (65%) was observed between the deduced amino acid sequences of the two enzymes, an apparent difference was observed at the C-terminal region: BGL1B has a 63-amino acid extension, which has no similarity with any known protein. Both recombinant enzymes expressed in Escherichia coli showed hydrolytic activity towards several beta-glycosidic compounds. However, the substrate recognition patterns of the two enzymes were quite different from each other. In particular, cellobiose was hydrolyzed more effectively by BGL1B than by BGL1A. The expression of the two genes in the fungus was monitored by reverse transcription-PCR, which showed that bgl1A was expressed constitutively in both glucose- and cellobiose-containing culture, whereas bgl1B was expressed in cellobiose culture but was repressed in glucose culture, possibly because of carbon catabolite repression. We conclude that BGL1B contributes to cellobiose metabolism during cellulose degradation by P. chrysosporium.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tsukada</LastName><ForeName>Takeshi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Yoshida</LastName><ForeName>Makoto</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AB253326</AccessionNumber><AccessionNumber>AB253327</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>08</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006027">Glycosides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012331">RNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>16462-44-5</RegistryNumber><NameOfSubstance UI="D002475">Cellobiose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002475" MajorTopicYN="N">Cellobiose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="Y">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006027" MajorTopicYN="N">Glycosides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012331" MajorTopicYN="N">RNA, Fungal</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>03</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>06</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>05</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>8</Month><Day>10</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>4</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>8</Month><Day>10</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16896601</ArticleId><ArticleId IdType="doi">10.1007/s00253-006-0526-z</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Tsukada, Takeshi" sort="Tsukada, Takeshi" uniqKey="Tsukada T" first="Takeshi" last="Tsukada">Takeshi Tsukada</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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