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...
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Veröffentlicht in: | Applied and Environmental Microbiology 1990-04, Vol.56 (4), p.1017-1024 |
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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 |
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(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&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> |
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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" |
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