Glycoside hydrolase inventory drives plant polysaccharide deconstruction by the extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus.
Identifieur interne : 002E52 ( Main/Exploration ); précédent : 002E51; suivant : 002E53Glycoside hydrolase inventory drives plant polysaccharide deconstruction by the extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus.
Auteurs : Amy L. Vanfossen [États-Unis] ; Inci Ozdemir ; Samantha L. Zelin ; Robert M. KellySource :
- Biotechnology and bioengineering [ 1097-0290 ] ; 2011.
Descripteurs français
- KwdFr :
- Analyse de profil d'expression de gènes (MeSH), Bactéries à Gram positif (enzymologie), Bactéries à Gram positif (génétique), Bactéries à Gram positif (métabolisme), Carboxyméthylcellulose de sodium (métabolisme), Glycosidases (composition chimique), Glycosidases (génétique), Glycosidases (métabolisme), Masse moléculaire (MeSH), Milieux de culture (composition chimique), Plantes (composition chimique), Polyosides (métabolisme), Protéines bactériennes (composition chimique), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Xylanes (métabolisme).
- MESH :
- composition chimique : Glycosidases, Milieux de culture, Plantes, Protéines bactériennes.
- enzymologie : Bactéries à Gram positif.
- génétique : Bactéries à Gram positif, Glycosidases, Protéines bactériennes.
- métabolisme : Bactéries à Gram positif, Carboxyméthylcellulose de sodium, Glycosidases, Polyosides, Protéines bactériennes, Xylanes.
- Analyse de profil d'expression de gènes, Masse moléculaire.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Carboxymethylcellulose Sodium (metabolism), Culture Media (chemistry), Gene Expression Profiling (MeSH), Glycoside Hydrolases (chemistry), Glycoside Hydrolases (genetics), Glycoside Hydrolases (metabolism), Gram-Positive Bacteria (enzymology), Gram-Positive Bacteria (genetics), Gram-Positive Bacteria (metabolism), Molecular Weight (MeSH), Plants (chemistry), Polysaccharides (metabolism), Xylans (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Culture Media, Glycoside Hydrolases.
- chemical , genetics : Bacterial Proteins, Glycoside Hydrolases.
- chemical , metabolism : Bacterial Proteins, Carboxymethylcellulose Sodium, Glycoside Hydrolases, Polysaccharides, Xylans.
- chemistry : Plants.
- enzymology : Gram-Positive Bacteria.
- genetics : Gram-Positive Bacteria.
- metabolism : Gram-Positive Bacteria.
- Gene Expression Profiling, Molecular Weight.
Abstract
The genome of Caldicellulosiruptor saccharolyticus encodes a range of glycoside hydrolases (GHs) that mediate plant biomass deconstruction by this bacterium. Two GH-based genomic loci that appear to be central to the hydrolysis of hemicellulosic and cellulosic substrates were examined. XynB-XynF (Csac_2404-Csac_2411) encodes intracellular and extracellular GHs that are active towards xylan and xylan side-chains, as well as carboxymethyl cellulose (CMC). XynD (Csac_2409) and XynE (Csac_2410) were produced recombinantly and confirmed to be xylanases. XynF (Csac_2411) was produced in two separate polypeptides, each with one GH43 catalytic domain displaying α-L-arabinofuranosidase activity. CelA-ManB (Csac_1076-Csac_1080) encodes four multi-domain, extracellular GHs, including CelB (Csac_1078), a 118 kDa extracellular enzyme not present in the other genome-sequenced member of this genus, Caldicellulosiruptor bescii (formerly Anaerocellum thermophilum). CelB contains both GH10 and GH5 domains, separated by a family 3 carbohydrate-binding module (CBM3). CelB encoded in Csac_1078 differed from the version originally reported (Saul et al., 1990, Appl Environ Microbiol 56:3117–3124) with respect to linker regions. CelB hydrolyzed xylan and CMC, as well as barley b-glucan, glucomannan, and arabinoxylan. For all substrates tested, intact CelB was significantly more active than either the individual GH5 and GH10 domains or the two discrete domains together, indicating that the multi-domain architecture is essential for complex carbohydrate hydrolysis. Transcriptomes for C. saccharolyticus grown at 70°C on glucose, xylose, xyloglucan, switchgrass, and poplar revealed that certain GHs were particularly responsive to growth on switchgrass and poplar and that CelB was in the top decile of all transcripts during growth on the plant biomass.
DOI: 10.1002/bit.23093
PubMed: 21337327
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Two GH-based genomic loci that appear to be central to the hydrolysis of hemicellulosic and cellulosic substrates were examined. XynB-XynF (Csac_2404-Csac_2411) encodes intracellular and extracellular GHs that are active towards xylan and xylan side-chains, as well as carboxymethyl cellulose (CMC). XynD (Csac_2409) and XynE (Csac_2410) were produced recombinantly and confirmed to be xylanases. XynF (Csac_2411) was produced in two separate polypeptides, each with one GH43 catalytic domain displaying α-L-arabinofuranosidase activity. CelA-ManB (Csac_1076-Csac_1080) encodes four multi-domain, extracellular GHs, including CelB (Csac_1078), a 118 kDa extracellular enzyme not present in the other genome-sequenced member of this genus, Caldicellulosiruptor bescii (formerly Anaerocellum thermophilum). CelB contains both GH10 and GH5 domains, separated by a family 3 carbohydrate-binding module (CBM3). CelB encoded in Csac_1078 differed from the version originally reported (Saul et al., 1990, Appl Environ Microbiol 56:3117–3124) with respect to linker regions. CelB hydrolyzed xylan and CMC, as well as barley b-glucan, glucomannan, and arabinoxylan. For all substrates tested, intact CelB was significantly more active than either the individual GH5 and GH10 domains or the two discrete domains together, indicating that the multi-domain architecture is essential for complex carbohydrate hydrolysis. Transcriptomes for C. saccharolyticus grown at 70°C on glucose, xylose, xyloglucan, switchgrass, and poplar revealed that certain GHs were particularly responsive to growth on switchgrass and poplar and that CelB was in the top decile of all transcripts during growth on the plant biomass.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21337327</PMID><DateCompleted><Year>2011</Year><Month>08</Month><Day>30</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1097-0290</ISSN><JournalIssue CitedMedium="Internet"><Volume>108</Volume><Issue>7</Issue><PubDate><Year>2011</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Biotechnology and bioengineering</Title><ISOAbbreviation>Biotechnol Bioeng</ISOAbbreviation></Journal><ArticleTitle>Glycoside hydrolase inventory drives plant polysaccharide deconstruction by the extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus.</ArticleTitle><Pagination><MedlinePgn>1559-69</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/bit.23093</ELocationID><Abstract><AbstractText>The genome of Caldicellulosiruptor saccharolyticus encodes a range of glycoside hydrolases (GHs) that mediate plant biomass deconstruction by this bacterium. Two GH-based genomic loci that appear to be central to the hydrolysis of hemicellulosic and cellulosic substrates were examined. XynB-XynF (Csac_2404-Csac_2411) encodes intracellular and extracellular GHs that are active towards xylan and xylan side-chains, as well as carboxymethyl cellulose (CMC). XynD (Csac_2409) and XynE (Csac_2410) were produced recombinantly and confirmed to be xylanases. XynF (Csac_2411) was produced in two separate polypeptides, each with one GH43 catalytic domain displaying α-L-arabinofuranosidase activity. CelA-ManB (Csac_1076-Csac_1080) encodes four multi-domain, extracellular GHs, including CelB (Csac_1078), a 118 kDa extracellular enzyme not present in the other genome-sequenced member of this genus, Caldicellulosiruptor bescii (formerly Anaerocellum thermophilum). CelB contains both GH10 and GH5 domains, separated by a family 3 carbohydrate-binding module (CBM3). CelB encoded in Csac_1078 differed from the version originally reported (Saul et al., 1990, Appl Environ Microbiol 56:3117–3124) with respect to linker regions. CelB hydrolyzed xylan and CMC, as well as barley b-glucan, glucomannan, and arabinoxylan. For all substrates tested, intact CelB was significantly more active than either the individual GH5 and GH10 domains or the two discrete domains together, indicating that the multi-domain architecture is essential for complex carbohydrate hydrolysis. Transcriptomes for C. saccharolyticus grown at 70°C on glucose, xylose, xyloglucan, switchgrass, and poplar revealed that certain GHs were particularly responsive to growth on switchgrass and poplar and that CelB was in the top decile of all transcripts during growth on the plant biomass.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>VanFossen</LastName><ForeName>Amy L</ForeName><Initials>AL</Initials><AffiliationInfo><Affiliation>Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ozdemir</LastName><ForeName>Inci</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Zelin</LastName><ForeName>Samantha L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Kelly</LastName><ForeName>Robert M</ForeName><Initials>RM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>03</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biotechnol Bioeng</MedlineTA><NlmUniqueID>7502021</NlmUniqueID><ISSNLinking>0006-3592</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003470">Culture Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020869" MajorTopicYN="N">Gene Expression Profiling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006094" MajorTopicYN="N">Gram-Positive Bacteria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>11</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>01</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>02</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>2</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>2</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>8</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21337327</ArticleId><ArticleId IdType="doi">10.1002/bit.23093</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><noCountry><name sortKey="Kelly, Robert M" sort="Kelly, Robert M" uniqKey="Kelly R" first="Robert M" last="Kelly">Robert M. Kelly</name><name sortKey="Ozdemir, Inci" sort="Ozdemir, Inci" uniqKey="Ozdemir I" first="Inci" last="Ozdemir">Inci Ozdemir</name><name sortKey="Zelin, Samantha L" sort="Zelin, Samantha L" uniqKey="Zelin S" first="Samantha L" last="Zelin">Samantha L. Zelin</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Vanfossen, Amy L" sort="Vanfossen, Amy L" uniqKey="Vanfossen A" first="Amy L" last="Vanfossen">Amy L. Vanfossen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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