Sequence, overproduction and purification of the family 11 endo-β-1,4-xylanase encoded by the xyl1 gene of Streptomyces sp. S38
The xyl1 gene encoding the Xyl1 xylanase of Streptomyces sp. strain S38 was cloned by screening an enriched DNA library with a specific DNA probe and sequenced. Three short 5 bp –CGAAA– sequences are located upstream of the Streptomyces sp. S38 xyl1 gene 105, 115 and 250 bp before the start codon. T...
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| Veröffentlicht in: | Gene 1999-09, Vol.237 (1), p.123-133 |
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| creator | Georis, Jacques Giannotta, Fabrizio Lamotte-Brasseur, Josette Devreese, Bart Van Beeumen, Jozef Granier, Benoı̂t Frère, Jean-Marie |
| description | The
xyl1 gene encoding the Xyl1 xylanase of
Streptomyces sp. strain S38 was cloned by screening an enriched DNA library with a specific DNA probe and sequenced. Three short 5
bp –CGAAA– sequences are located upstream of the
Streptomyces sp. S38
xyl1 gene 105, 115 and 250
bp before the start codon. These sequences, named boxes 1, 2 and 3, are conserved upstream of the Actinomycetales xylanase genes and are specifically recognized by a DNA-binding protein (Giannotta et al., 1994. FEMS Microbiol. Lett. 142, 91–97) and could be probably involved in the regulation of xylanase production. The Xyl1 ORF encodes a 228 residue polypeptide and the Xyl1 preprotein contains a 38 residue signal peptide whose cleavage yields a 190 residue mature protein of calculated
M
r=20
585 and basic p
I value of 9.12. The molecular mass of the produced and purified mature protein determined by mass spectrometry (20
586±1
Da) and its p
I (9.8) agree with these calculated values. Its N-terminal amino-acid sequence confirmed the proposed cleavage site between the signal peptide and the mature protein. Comparisons between Xyl1 and the 62 other xylanases belonging to family 11 allowed the construction of a phylogenetic tree and revealed its close relationship with Actinomycetales enzymes. Moreover, nine residues were found to be strictly conserved among the 63 xylanases. |
| doi_str_mv | 10.1016/S0378-1119(99)00311-X |
| format | Article |
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xyl1 gene encoding the Xyl1 xylanase of
Streptomyces sp. strain S38 was cloned by screening an enriched DNA library with a specific DNA probe and sequenced. Three short 5
bp –CGAAA– sequences are located upstream of the
Streptomyces sp. S38
xyl1 gene 105, 115 and 250
bp before the start codon. These sequences, named boxes 1, 2 and 3, are conserved upstream of the Actinomycetales xylanase genes and are specifically recognized by a DNA-binding protein (Giannotta et al., 1994. FEMS Microbiol. Lett. 142, 91–97) and could be probably involved in the regulation of xylanase production. The Xyl1 ORF encodes a 228 residue polypeptide and the Xyl1 preprotein contains a 38 residue signal peptide whose cleavage yields a 190 residue mature protein of calculated
M
r=20
585 and basic p
I value of 9.12. The molecular mass of the produced and purified mature protein determined by mass spectrometry (20
586±1
Da) and its p
I (9.8) agree with these calculated values. Its N-terminal amino-acid sequence confirmed the proposed cleavage site between the signal peptide and the mature protein. Comparisons between Xyl1 and the 62 other xylanases belonging to family 11 allowed the construction of a phylogenetic tree and revealed its close relationship with Actinomycetales enzymes. Moreover, nine residues were found to be strictly conserved among the 63 xylanases.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/S0378-1119(99)00311-X</identifier><identifier>PMID: 10524243</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; endo-1,4-b-xylanase ; Endo-1,4-beta Xylanases ; endo-^b-1,4-xylanase ; Gene cloning ; Gene expression ; Glycolyl-hydrolase ; Molecular Sequence Data ; Phylogenetic relationship ; Phylogeny ; Plasmids - genetics ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Regulation ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Species Specificity ; Streptomyces ; Streptomyces - enzymology ; xyl1 gene ; Xylosidases - genetics ; Xylosidases - isolation & purification ; Xylosidases - metabolism</subject><ispartof>Gene, 1999-09, Vol.237 (1), p.123-133</ispartof><rights>1999 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-2cd9aafcf12563864dbc0c3a953297227aa0724a768ca864ca53d96ba57c86e73</citedby><cites>FETCH-LOGICAL-c392t-2cd9aafcf12563864dbc0c3a953297227aa0724a768ca864ca53d96ba57c86e73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0378-1119(99)00311-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10524243$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Georis, Jacques</creatorcontrib><creatorcontrib>Giannotta, Fabrizio</creatorcontrib><creatorcontrib>Lamotte-Brasseur, Josette</creatorcontrib><creatorcontrib>Devreese, Bart</creatorcontrib><creatorcontrib>Van Beeumen, Jozef</creatorcontrib><creatorcontrib>Granier, Benoı̂t</creatorcontrib><creatorcontrib>Frère, Jean-Marie</creatorcontrib><title>Sequence, overproduction and purification of the family 11 endo-β-1,4-xylanase encoded by the xyl1 gene of Streptomyces sp. S38</title><title>Gene</title><addtitle>Gene</addtitle><description>The
xyl1 gene encoding the Xyl1 xylanase of
Streptomyces sp. strain S38 was cloned by screening an enriched DNA library with a specific DNA probe and sequenced. Three short 5
bp –CGAAA– sequences are located upstream of the
Streptomyces sp. S38
xyl1 gene 105, 115 and 250
bp before the start codon. These sequences, named boxes 1, 2 and 3, are conserved upstream of the Actinomycetales xylanase genes and are specifically recognized by a DNA-binding protein (Giannotta et al., 1994. FEMS Microbiol. Lett. 142, 91–97) and could be probably involved in the regulation of xylanase production. The Xyl1 ORF encodes a 228 residue polypeptide and the Xyl1 preprotein contains a 38 residue signal peptide whose cleavage yields a 190 residue mature protein of calculated
M
r=20
585 and basic p
I value of 9.12. The molecular mass of the produced and purified mature protein determined by mass spectrometry (20
586±1
Da) and its p
I (9.8) agree with these calculated values. Its N-terminal amino-acid sequence confirmed the proposed cleavage site between the signal peptide and the mature protein. Comparisons between Xyl1 and the 62 other xylanases belonging to family 11 allowed the construction of a phylogenetic tree and revealed its close relationship with Actinomycetales enzymes. Moreover, nine residues were found to be strictly conserved among the 63 xylanases.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>endo-1,4-b-xylanase</subject><subject>Endo-1,4-beta Xylanases</subject><subject>endo-^b-1,4-xylanase</subject><subject>Gene cloning</subject><subject>Gene expression</subject><subject>Glycolyl-hydrolase</subject><subject>Molecular Sequence Data</subject><subject>Phylogenetic relationship</subject><subject>Phylogeny</subject><subject>Plasmids - genetics</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Regulation</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><subject>Streptomyces</subject><subject>Streptomyces - enzymology</subject><subject>xyl1 gene</subject><subject>Xylosidases - genetics</subject><subject>Xylosidases - isolation & purification</subject><subject>Xylosidases - metabolism</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9uFSEUxonR2NvqI2hYmZqUyoH5AytjGqsmTbq4NemOcOGMYu4MI8w0nZ3P5IP4THLvbYy7siF8_L5zOHyEvAJ-Dhyad2suW8UAQJ9q_ZZzCcBun5AVqFazclRPyeofckSOc_7By6pr8ZwcAa9FJSq5Ir_W-HPGweEZjXeYxhT97KYQB2oHT8c5hS44uxdiR6fvSDvbh-1CASgOPrI_vxmcVex-2drBZiyiix493Sx7uuhAv-GAO_t6SjhOsV8cZprHc7qW6gV51tltxpcP-wn5evnx5uIzu7r-9OXiwxVzUouJCee1tZ3rQNSNVE3lN447aXUthW6FaK3lrahs2yhny7WztfS62di6darBVp6QN4e6ZcQycZ5MH7LDbXk2xjmblitomoo_CoKS0AglC1gfQJdizgk7M6bQ27QY4GaXkdlnZHYBGK3NPiNzW3yvHxrMmx79f65DKAV4fwCw_MddwGSyC7uMfEjoJuNjeKTFX4FRoWw</recordid><startdate>19990903</startdate><enddate>19990903</enddate><creator>Georis, Jacques</creator><creator>Giannotta, Fabrizio</creator><creator>Lamotte-Brasseur, Josette</creator><creator>Devreese, Bart</creator><creator>Van Beeumen, Jozef</creator><creator>Granier, Benoı̂t</creator><creator>Frère, Jean-Marie</creator><general>Elsevier B.V</general><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19990903</creationdate><title>Sequence, overproduction and purification of the family 11 endo-β-1,4-xylanase encoded by the xyl1 gene of Streptomyces sp. S38</title><author>Georis, Jacques ; Giannotta, Fabrizio ; Lamotte-Brasseur, Josette ; Devreese, Bart ; Van Beeumen, Jozef ; Granier, Benoı̂t ; Frère, Jean-Marie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-2cd9aafcf12563864dbc0c3a953297227aa0724a768ca864ca53d96ba57c86e73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>endo-1,4-b-xylanase</topic><topic>Endo-1,4-beta Xylanases</topic><topic>endo-^b-1,4-xylanase</topic><topic>Gene cloning</topic><topic>Gene expression</topic><topic>Glycolyl-hydrolase</topic><topic>Molecular Sequence Data</topic><topic>Phylogenetic relationship</topic><topic>Phylogeny</topic><topic>Plasmids - genetics</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Regulation</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><topic>Streptomyces</topic><topic>Streptomyces - enzymology</topic><topic>xyl1 gene</topic><topic>Xylosidases - genetics</topic><topic>Xylosidases - isolation & purification</topic><topic>Xylosidases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Georis, Jacques</creatorcontrib><creatorcontrib>Giannotta, Fabrizio</creatorcontrib><creatorcontrib>Lamotte-Brasseur, Josette</creatorcontrib><creatorcontrib>Devreese, Bart</creatorcontrib><creatorcontrib>Van Beeumen, Jozef</creatorcontrib><creatorcontrib>Granier, Benoı̂t</creatorcontrib><creatorcontrib>Frère, Jean-Marie</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Georis, Jacques</au><au>Giannotta, Fabrizio</au><au>Lamotte-Brasseur, Josette</au><au>Devreese, Bart</au><au>Van Beeumen, Jozef</au><au>Granier, Benoı̂t</au><au>Frère, Jean-Marie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sequence, overproduction and purification of the family 11 endo-β-1,4-xylanase encoded by the xyl1 gene of Streptomyces sp. S38</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>1999-09-03</date><risdate>1999</risdate><volume>237</volume><issue>1</issue><spage>123</spage><epage>133</epage><pages>123-133</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>The
xyl1 gene encoding the Xyl1 xylanase of
Streptomyces sp. strain S38 was cloned by screening an enriched DNA library with a specific DNA probe and sequenced. Three short 5
bp –CGAAA– sequences are located upstream of the
Streptomyces sp. S38
xyl1 gene 105, 115 and 250
bp before the start codon. These sequences, named boxes 1, 2 and 3, are conserved upstream of the Actinomycetales xylanase genes and are specifically recognized by a DNA-binding protein (Giannotta et al., 1994. FEMS Microbiol. Lett. 142, 91–97) and could be probably involved in the regulation of xylanase production. The Xyl1 ORF encodes a 228 residue polypeptide and the Xyl1 preprotein contains a 38 residue signal peptide whose cleavage yields a 190 residue mature protein of calculated
M
r=20
585 and basic p
I value of 9.12. The molecular mass of the produced and purified mature protein determined by mass spectrometry (20
586±1
Da) and its p
I (9.8) agree with these calculated values. Its N-terminal amino-acid sequence confirmed the proposed cleavage site between the signal peptide and the mature protein. Comparisons between Xyl1 and the 62 other xylanases belonging to family 11 allowed the construction of a phylogenetic tree and revealed its close relationship with Actinomycetales enzymes. Moreover, nine residues were found to be strictly conserved among the 63 xylanases.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>10524243</pmid><doi>10.1016/S0378-1119(99)00311-X</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1119 |
| ispartof | Gene, 1999-09, Vol.237 (1), p.123-133 |
| issn | 0378-1119 1879-0038 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70816640 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Base Sequence Cloning, Molecular endo-1,4-b-xylanase Endo-1,4-beta Xylanases endo-^b-1,4-xylanase Gene cloning Gene expression Glycolyl-hydrolase Molecular Sequence Data Phylogenetic relationship Phylogeny Plasmids - genetics Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Regulation Sequence Analysis, DNA Sequence Homology, Amino Acid Species Specificity Streptomyces Streptomyces - enzymology xyl1 gene Xylosidases - genetics Xylosidases - isolation & purification Xylosidases - metabolism |
| title | Sequence, overproduction and purification of the family 11 endo-β-1,4-xylanase encoded by the xyl1 gene of Streptomyces sp. S38 |
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