Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum"

A lambda recombinant bacteriophage coding for xylanase and beta-xylosidase activity has been isolated from a genomic library of the extremely thermophilic anaerobe "Caldocellum saccharolyticum." Partial Sau3AI fragments of the lambda recombinant DNA were ligated into pBR322. A recombinant...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Applied and Environmental Microbiology 1990-04, Vol.56 (4), p.1017-1024
Hauptverfasser: Luthi, E. (University of Auckland, Auckland, New Zealand), Love, D.R, McAnulty, J, Wallace, C, Caughey, P.A, Saul, D, Bergquist, P.L
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1024
container_issue 4
container_start_page 1017
container_title Applied and Environmental Microbiology
container_volume 56
creator Luthi, E. (University of Auckland, Auckland, New Zealand)
Love, D.R
McAnulty, J
Wallace, C
Caughey, P.A
Saul, D
Bergquist, P.L
description A lambda recombinant bacteriophage coding for xylanase and beta-xylosidase activity has been isolated from a genomic library of the extremely thermophilic anaerobe "Caldocellum saccharolyticum." Partial Sau3AI fragments of the lambda recombinant DNA were ligated into pBR322. A recombinant plasmid with an insertion of ca. 7 kilobases of thermophilic DNA expressing both enzymatic activities was isolated. The location of the genes has been established by analyzing deletion derivatives, and the DNA sequence of 6.067 kilobases of the insert has been determined. Five open reading frames (ORFS) were found, one of which (ORF1; Mr 40,455) appears to code for a xylanase (XynA) which also acts on o-nitrophenyl-beta-D-xylopyranoside. Another, ORF5 (Mr 56,365), codes for a beta-xylosidase (XynB). The xynA gene product shows significant homology with the xylanases from the alkalophilic Bacillus sp. strain C125 and Clostridium thermocellum
doi_str_mv 10.1128/aem.56.4.1017-1024.1990
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_184337</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>79775943</sourcerecordid><originalsourceid>FETCH-LOGICAL-c642t-324dab8fd3f005a713583a0b5b56eb630612918f7555680048c88040d13479983</originalsourceid><addsrcrecordid>eNpVUU1v1DAQtRCoLAt_AAmRVoJTs9hxHNsHDmjFl1SJA_RsTRwnMXLsxc5Clz_A38bprgq1ZHlG896bGT-EXhK8IaQSb8BMG9Zs6g3BhJcEVzmSEj9AK4KlKBmlzUO0wljKsqpq_Bg9Sek7xrjGjThDZxW5PSv0Z-uCt364LJL5sTdemwI8uEOy6TJHXWFudtGkZIMvQl8MxptUZFjoMqm4OTjwZWeGCLe58b8PUwb0MUzFPJrlxinsRutMcbEF1wVtnNtPRQKtR4jBHWar99PFU_SoB5fMs9O7Rtcf3n_bfiqvvnz8vH13VeqmruaSVnUHreg72mPMgBPKBAXcspY1pm0obkglieg5Y6wReV2hhchLd4TWXEpB1-jtUXe3byfTaePnCE7top0gHlQAq-5XvB3VEH4qImpKeea_PvFjyP-VZjXZtOwE3oR9UlxyzmSGrhE_AnUMKUXT3_UgWC0WqmyhYo2q1WKhWixUi4WZ-eL_Ee94J89y_dWpDkmD6yN4bdM_eclrzvGic37EjXYYf9loFKTpfteMeX7E9BAUDDHrXH_NM9RUSvoXNSy7Gg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79775943</pqid></control><display><type>article</type><title>Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum"</title><source>American Society for Microbiology</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Luthi, E. (University of Auckland, Auckland, New Zealand) ; Love, D.R ; McAnulty, J ; Wallace, C ; Caughey, P.A ; Saul, D ; Bergquist, P.L</creator><creatorcontrib>Luthi, E. (University of Auckland, Auckland, New Zealand) ; Love, D.R ; McAnulty, J ; Wallace, C ; Caughey, P.A ; Saul, D ; Bergquist, P.L</creatorcontrib><description>A lambda recombinant bacteriophage coding for xylanase and beta-xylosidase activity has been isolated from a genomic library of the extremely thermophilic anaerobe "Caldocellum saccharolyticum." Partial Sau3AI fragments of the lambda recombinant DNA were ligated into pBR322. A recombinant plasmid with an insertion of ca. 7 kilobases of thermophilic DNA expressing both enzymatic activities was isolated. The location of the genes has been established by analyzing deletion derivatives, and the DNA sequence of 6.067 kilobases of the insert has been determined. Five open reading frames (ORFS) were found, one of which (ORF1; Mr 40,455) appears to code for a xylanase (XynA) which also acts on o-nitrophenyl-beta-D-xylopyranoside. Another, ORF5 (Mr 56,365), codes for a beta-xylosidase (XynB). The xynA gene product shows significant homology with the xylanases from the alkalophilic Bacillus sp. strain C125 and Clostridium thermocellum</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/aem.56.4.1017-1024.1990</identifier><identifier>PMID: 2111111</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Amino Acid Sequence ; BACTERIA ; Bacteria, Anaerobic - enzymology ; Bacteria, Anaerobic - genetics ; BACTERIE ; BACTERIOFAGOS ; BACTERIOPHAGE ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Cloning, Molecular ; DNA, Bacterial - genetics ; ENZIMAS ; ENZYME ; Fundamental and applied biological sciences. Psychology ; GENE ; GENES ; Genes, Bacterial ; Genetic engineering ; Genetic technics ; Glycoside Hydrolases - genetics ; HIDROLASAS ; HYDROLASE ; Methods. Procedures. Technologies ; MICROORGANISME THERMOPHILE ; MICROORGANISMOS TERMOFILOS ; Molecular cloning ; Molecular Sequence Data ; NUCLEOTIDE ; NUCLEOTIDOS ; Promoter Regions, Genetic ; Protein Sorting Signals - genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Temperature ; XILANOS ; Xylan Endo-1,3-beta-Xylosidase ; XYLANE ; Xylosidases - genetics</subject><ispartof>Applied and Environmental Microbiology, 1990-04, Vol.56 (4), p.1017-1024</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c642t-324dab8fd3f005a713583a0b5b56eb630612918f7555680048c88040d13479983</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC184337/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC184337/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3175,3176,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=19747700$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2111111$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Luthi, E. (University of Auckland, Auckland, New Zealand)</creatorcontrib><creatorcontrib>Love, D.R</creatorcontrib><creatorcontrib>McAnulty, J</creatorcontrib><creatorcontrib>Wallace, C</creatorcontrib><creatorcontrib>Caughey, P.A</creatorcontrib><creatorcontrib>Saul, D</creatorcontrib><creatorcontrib>Bergquist, P.L</creatorcontrib><title>Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum"</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>A lambda recombinant bacteriophage coding for xylanase and beta-xylosidase activity has been isolated from a genomic library of the extremely thermophilic anaerobe "Caldocellum saccharolyticum." Partial Sau3AI fragments of the lambda recombinant DNA were ligated into pBR322. A recombinant plasmid with an insertion of ca. 7 kilobases of thermophilic DNA expressing both enzymatic activities was isolated. The location of the genes has been established by analyzing deletion derivatives, and the DNA sequence of 6.067 kilobases of the insert has been determined. Five open reading frames (ORFS) were found, one of which (ORF1; Mr 40,455) appears to code for a xylanase (XynA) which also acts on o-nitrophenyl-beta-D-xylopyranoside. Another, ORF5 (Mr 56,365), codes for a beta-xylosidase (XynB). The xynA gene product shows significant homology with the xylanases from the alkalophilic Bacillus sp. strain C125 and Clostridium thermocellum</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Amino Acid Sequence</subject><subject>BACTERIA</subject><subject>Bacteria, Anaerobic - enzymology</subject><subject>Bacteria, Anaerobic - genetics</subject><subject>BACTERIE</subject><subject>BACTERIOFAGOS</subject><subject>BACTERIOPHAGE</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial - genetics</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE</subject><subject>GENES</subject><subject>Genes, Bacterial</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Glycoside Hydrolases - genetics</subject><subject>HIDROLASAS</subject><subject>HYDROLASE</subject><subject>Methods. Procedures. Technologies</subject><subject>MICROORGANISME THERMOPHILE</subject><subject>MICROORGANISMOS TERMOFILOS</subject><subject>Molecular cloning</subject><subject>Molecular Sequence Data</subject><subject>NUCLEOTIDE</subject><subject>NUCLEOTIDOS</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Sorting Signals - genetics</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Temperature</subject><subject>XILANOS</subject><subject>Xylan Endo-1,3-beta-Xylosidase</subject><subject>XYLANE</subject><subject>Xylosidases - genetics</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUU1v1DAQtRCoLAt_AAmRVoJTs9hxHNsHDmjFl1SJA_RsTRwnMXLsxc5Clz_A38bprgq1ZHlG896bGT-EXhK8IaQSb8BMG9Zs6g3BhJcEVzmSEj9AK4KlKBmlzUO0wljKsqpq_Bg9Sek7xrjGjThDZxW5PSv0Z-uCt364LJL5sTdemwI8uEOy6TJHXWFudtGkZIMvQl8MxptUZFjoMqm4OTjwZWeGCLe58b8PUwb0MUzFPJrlxinsRutMcbEF1wVtnNtPRQKtR4jBHWar99PFU_SoB5fMs9O7Rtcf3n_bfiqvvnz8vH13VeqmruaSVnUHreg72mPMgBPKBAXcspY1pm0obkglieg5Y6wReV2hhchLd4TWXEpB1-jtUXe3byfTaePnCE7top0gHlQAq-5XvB3VEH4qImpKeea_PvFjyP-VZjXZtOwE3oR9UlxyzmSGrhE_AnUMKUXT3_UgWC0WqmyhYo2q1WKhWixUi4WZ-eL_Ee94J89y_dWpDkmD6yN4bdM_eclrzvGic37EjXYYf9loFKTpfteMeX7E9BAUDDHrXH_NM9RUSvoXNSy7Gg</recordid><startdate>19900401</startdate><enddate>19900401</enddate><creator>Luthi, E. (University of Auckland, Auckland, New Zealand)</creator><creator>Love, D.R</creator><creator>McAnulty, J</creator><creator>Wallace, C</creator><creator>Caughey, P.A</creator><creator>Saul, D</creator><creator>Bergquist, P.L</creator><general>American Society for Microbiology</general><scope>FBQ</scope><scope>IQODW</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19900401</creationdate><title>Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum"</title><author>Luthi, E. (University of Auckland, Auckland, New Zealand) ; Love, D.R ; McAnulty, J ; Wallace, C ; Caughey, P.A ; Saul, D ; Bergquist, P.L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c642t-324dab8fd3f005a713583a0b5b56eb630612918f7555680048c88040d13479983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Amino Acid Sequence</topic><topic>BACTERIA</topic><topic>Bacteria, Anaerobic - enzymology</topic><topic>Bacteria, Anaerobic - genetics</topic><topic>BACTERIE</topic><topic>BACTERIOFAGOS</topic><topic>BACTERIOPHAGE</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial - genetics</topic><topic>ENZIMAS</topic><topic>ENZYME</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE</topic><topic>GENES</topic><topic>Genes, Bacterial</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Glycoside Hydrolases - genetics</topic><topic>HIDROLASAS</topic><topic>HYDROLASE</topic><topic>Methods. Procedures. Technologies</topic><topic>MICROORGANISME THERMOPHILE</topic><topic>MICROORGANISMOS TERMOFILOS</topic><topic>Molecular cloning</topic><topic>Molecular Sequence Data</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDOS</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Sorting Signals - genetics</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Temperature</topic><topic>XILANOS</topic><topic>Xylan Endo-1,3-beta-Xylosidase</topic><topic>XYLANE</topic><topic>Xylosidases - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Luthi, E. (University of Auckland, Auckland, New Zealand)</creatorcontrib><creatorcontrib>Love, D.R</creatorcontrib><creatorcontrib>McAnulty, J</creatorcontrib><creatorcontrib>Wallace, C</creatorcontrib><creatorcontrib>Caughey, P.A</creatorcontrib><creatorcontrib>Saul, D</creatorcontrib><creatorcontrib>Bergquist, P.L</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Luthi, E. (University of Auckland, Auckland, New Zealand)</au><au>Love, D.R</au><au>McAnulty, J</au><au>Wallace, C</au><au>Caughey, P.A</au><au>Saul, D</au><au>Bergquist, P.L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum"</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>1990-04-01</date><risdate>1990</risdate><volume>56</volume><issue>4</issue><spage>1017</spage><epage>1024</epage><pages>1017-1024</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>A lambda recombinant bacteriophage coding for xylanase and beta-xylosidase activity has been isolated from a genomic library of the extremely thermophilic anaerobe "Caldocellum saccharolyticum." Partial Sau3AI fragments of the lambda recombinant DNA were ligated into pBR322. A recombinant plasmid with an insertion of ca. 7 kilobases of thermophilic DNA expressing both enzymatic activities was isolated. The location of the genes has been established by analyzing deletion derivatives, and the DNA sequence of 6.067 kilobases of the insert has been determined. Five open reading frames (ORFS) were found, one of which (ORF1; Mr 40,455) appears to code for a xylanase (XynA) which also acts on o-nitrophenyl-beta-D-xylopyranoside. Another, ORF5 (Mr 56,365), codes for a beta-xylosidase (XynB). The xynA gene product shows significant homology with the xylanases from the alkalophilic Bacillus sp. strain C125 and Clostridium thermocellum</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>2111111</pmid><doi>10.1128/aem.56.4.1017-1024.1990</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0099-2240
ispartof Applied and Environmental Microbiology, 1990-04, Vol.56 (4), p.1017-1024
issn 0099-2240
1098-5336
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_184337
source American Society for Microbiology; MEDLINE; PubMed Central; Alma/SFX Local Collection
subjects ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Amino Acid Sequence
BACTERIA
Bacteria, Anaerobic - enzymology
Bacteria, Anaerobic - genetics
BACTERIE
BACTERIOFAGOS
BACTERIOPHAGE
Base Sequence
Biological and medical sciences
Biotechnology
Cloning, Molecular
DNA, Bacterial - genetics
ENZIMAS
ENZYME
Fundamental and applied biological sciences. Psychology
GENE
GENES
Genes, Bacterial
Genetic engineering
Genetic technics
Glycoside Hydrolases - genetics
HIDROLASAS
HYDROLASE
Methods. Procedures. Technologies
MICROORGANISME THERMOPHILE
MICROORGANISMOS TERMOFILOS
Molecular cloning
Molecular Sequence Data
NUCLEOTIDE
NUCLEOTIDOS
Promoter Regions, Genetic
Protein Sorting Signals - genetics
Restriction Mapping
Sequence Homology, Nucleic Acid
Temperature
XILANOS
Xylan Endo-1,3-beta-Xylosidase
XYLANE
Xylosidases - genetics
title Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum"
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T14%3A55%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cloning,%20sequence%20analysis,%20and%20expression%20of%20genes%20encoding%20xylan-degrading%20enzymes%20from%20the%20thermophile%20%22Caldocellum%20saccharolyticum%22&rft.jtitle=Applied%20and%20Environmental%20Microbiology&rft.au=Luthi,%20E.%20(University%20of%20Auckland,%20Auckland,%20New%20Zealand)&rft.date=1990-04-01&rft.volume=56&rft.issue=4&rft.spage=1017&rft.epage=1024&rft.pages=1017-1024&rft.issn=0099-2240&rft.eissn=1098-5336&rft.coden=AEMIDF&rft_id=info:doi/10.1128/aem.56.4.1017-1024.1990&rft_dat=%3Cproquest_pubme%3E79775943%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=79775943&rft_id=info:pmid/2111111&rfr_iscdi=true