Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)
Abstract The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N′-diacetylchitobiose [(GlcNAc)2] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and ass...
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| Veröffentlicht in: | FEMS microbiology letters 2013-03, Vol.340 (1), p.33-40 |
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| creator | Saito, Akihiro Ebise, Hiroki Orihara, Yukari Murakami, Satoshi Sano, Yukari Kimura, Akane Sugiyama, Yuuta Ando, Akikazu Fujii, Takeshi Miyashita, Kiyotaka |
| description | Abstract
The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N′-diacetylchitobiose [(GlcNAc)2] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and assimilation of chitin, we obtained and characterized a recombinant DasD protein and a dasD-null mutant of S. coelicolor A3(2). The recombinant DasD protein produced in Escherichia coli showed N-acetyl-β-d-glucosaminidase (GlcNAcase) activity and its optimum temperature and pH were 40 °C and 7, respectively. dasD transcription was strongly induced in the presence of chitin, weakly by chitosan, but not by cellulose or xylan in S. coelicolor A3(2). Immuno-blot analysis demonstrated that DasD is a cytoplasmic protein. The dasD-null mutant exhibited cellular GlcNAcase activity which was comparable with that of the parent strain M145. DasD, thus, did not seem to be a major GlcNAcase. Induced extracellular chitinase activity in the dasD-null mutant was, interestingly, higher than M145, in the presence of colloidal chitin or (GlcNAc)2. In contrast to M145, (GlcNAc)2 temporally accumulated in the culture supernatant of the dasD-null mutant in the presence of colloidal chitin. |
| doi_str_mv | 10.1111/1574-6968.12069 |
| format | Article |
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The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N′-diacetylchitobiose [(GlcNAc)2] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and assimilation of chitin, we obtained and characterized a recombinant DasD protein and a dasD-null mutant of S. coelicolor A3(2). The recombinant DasD protein produced in Escherichia coli showed N-acetyl-β-d-glucosaminidase (GlcNAcase) activity and its optimum temperature and pH were 40 °C and 7, respectively. dasD transcription was strongly induced in the presence of chitin, weakly by chitosan, but not by cellulose or xylan in S. coelicolor A3(2). Immuno-blot analysis demonstrated that DasD is a cytoplasmic protein. The dasD-null mutant exhibited cellular GlcNAcase activity which was comparable with that of the parent strain M145. DasD, thus, did not seem to be a major GlcNAcase. Induced extracellular chitinase activity in the dasD-null mutant was, interestingly, higher than M145, in the presence of colloidal chitin or (GlcNAc)2. In contrast to M145, (GlcNAc)2 temporally accumulated in the culture supernatant of the dasD-null mutant in the presence of colloidal chitin.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/1574-6968.12069</identifier><identifier>PMID: 23278377</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Acetylglucosaminidase - genetics ; Acetylglucosaminidase - metabolism ; actinomycetes ; Bacteriology ; Biological and medical sciences ; Chitin - metabolism ; chitinase ; chitobiase ; Cloning, Molecular ; Cytoplasm - enzymology ; Enzyme Stability ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Gene Deletion ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; GH family 3 ; glycoside hydrolase ; Hydrogen-Ion Concentration ; Microbiology ; Miscellaneous ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Streptomyces coelicolor ; Streptomyces coelicolor - enzymology ; Streptomyces coelicolor - genetics ; Streptomyces coelicolor - metabolism ; Temperature</subject><ispartof>FEMS microbiology letters, 2013-03, Vol.340 (1), p.33-40</ispartof><rights>2013 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2013</rights><rights>2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2014 INIST-CNRS</rights><rights>2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4419-5e416737317e130f8a0da12241c85075d9b0b2a6ea5cd7524793b2ce6a5156b43</citedby><cites>FETCH-LOGICAL-c4419-5e416737317e130f8a0da12241c85075d9b0b2a6ea5cd7524793b2ce6a5156b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2F1574-6968.12069$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1574-6968.12069$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26903780$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23278377$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Saito, Akihiro</creatorcontrib><creatorcontrib>Ebise, Hiroki</creatorcontrib><creatorcontrib>Orihara, Yukari</creatorcontrib><creatorcontrib>Murakami, Satoshi</creatorcontrib><creatorcontrib>Sano, Yukari</creatorcontrib><creatorcontrib>Kimura, Akane</creatorcontrib><creatorcontrib>Sugiyama, Yuuta</creatorcontrib><creatorcontrib>Ando, Akikazu</creatorcontrib><creatorcontrib>Fujii, Takeshi</creatorcontrib><creatorcontrib>Miyashita, Kiyotaka</creatorcontrib><title>Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N′-diacetylchitobiose [(GlcNAc)2] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and assimilation of chitin, we obtained and characterized a recombinant DasD protein and a dasD-null mutant of S. coelicolor A3(2). The recombinant DasD protein produced in Escherichia coli showed N-acetyl-β-d-glucosaminidase (GlcNAcase) activity and its optimum temperature and pH were 40 °C and 7, respectively. dasD transcription was strongly induced in the presence of chitin, weakly by chitosan, but not by cellulose or xylan in S. coelicolor A3(2). Immuno-blot analysis demonstrated that DasD is a cytoplasmic protein. The dasD-null mutant exhibited cellular GlcNAcase activity which was comparable with that of the parent strain M145. DasD, thus, did not seem to be a major GlcNAcase. Induced extracellular chitinase activity in the dasD-null mutant was, interestingly, higher than M145, in the presence of colloidal chitin or (GlcNAc)2. In contrast to M145, (GlcNAc)2 temporally accumulated in the culture supernatant of the dasD-null mutant in the presence of colloidal chitin.</description><subject>Acetylglucosaminidase - genetics</subject><subject>Acetylglucosaminidase - metabolism</subject><subject>actinomycetes</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Chitin - metabolism</subject><subject>chitinase</subject><subject>chitobiase</subject><subject>Cloning, Molecular</subject><subject>Cytoplasm - enzymology</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Deletion</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>GH family 3</subject><subject>glycoside hydrolase</subject><subject>Hydrogen-Ion Concentration</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Streptomyces coelicolor</subject><subject>Streptomyces coelicolor - enzymology</subject><subject>Streptomyces coelicolor - genetics</subject><subject>Streptomyces coelicolor - metabolism</subject><subject>Temperature</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EokNhzQ55g1SQ3PonjpNl1R9AGmABrKMb52ZqlMSDnRSl78DL8CA8Ew4zLSyQ6o0t3-8c3-tDyHPBj0VaJ0KbjOVlXhwLyfPyAVnd3TwkK65MwQQvzQF5EuNXznmWqMfkQCppCmXMivy4GG7mHkZnKQwN3eCAy9leQQA7YnA3qeYH6ls6XiE9h3hOt8GP6Aa69TFijG7Y0A8MLI5zx379ZA3bdJP1EXo3uAYi0uTkrt040yT6NAbcjr6fLUZqPXbO-s4HeqqO5Kun5FELXcRn-_2QfLm8-Hz2lq0_vnl3drpmNstEyTRmIjfKKGFQKN4WwBsQUmbCFpob3ZQ1ryXkCNo2RsvMlKqWFnPQQud1pg7J0c43jfJtwjhWvYsWuw4G9FOshEqcUFqp-1FZZLLQhVpcT3aoDelnArbVNrgewlwJXi1xVUs41RJO9SeupHixN5_qHps7_jafBLzcAxAtdG2Awbr4l8vLJWOeOL3jvrsO5_verS7fr28beL3T-Wn7XxX7p9vfQDq5Uw</recordid><startdate>201303</startdate><enddate>201303</enddate><creator>Saito, Akihiro</creator><creator>Ebise, Hiroki</creator><creator>Orihara, Yukari</creator><creator>Murakami, Satoshi</creator><creator>Sano, Yukari</creator><creator>Kimura, Akane</creator><creator>Sugiyama, Yuuta</creator><creator>Ando, Akikazu</creator><creator>Fujii, Takeshi</creator><creator>Miyashita, Kiyotaka</creator><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>201303</creationdate><title>Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)</title><author>Saito, Akihiro ; Ebise, Hiroki ; Orihara, Yukari ; Murakami, Satoshi ; Sano, Yukari ; Kimura, Akane ; Sugiyama, Yuuta ; Ando, Akikazu ; Fujii, Takeshi ; Miyashita, Kiyotaka</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4419-5e416737317e130f8a0da12241c85075d9b0b2a6ea5cd7524793b2ce6a5156b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acetylglucosaminidase - genetics</topic><topic>Acetylglucosaminidase - metabolism</topic><topic>actinomycetes</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Chitin - metabolism</topic><topic>chitinase</topic><topic>chitobiase</topic><topic>Cloning, Molecular</topic><topic>Cytoplasm - enzymology</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Deletion</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>GH family 3</topic><topic>glycoside hydrolase</topic><topic>Hydrogen-Ion Concentration</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Streptomyces coelicolor</topic><topic>Streptomyces coelicolor - enzymology</topic><topic>Streptomyces coelicolor - genetics</topic><topic>Streptomyces coelicolor - metabolism</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saito, Akihiro</creatorcontrib><creatorcontrib>Ebise, Hiroki</creatorcontrib><creatorcontrib>Orihara, Yukari</creatorcontrib><creatorcontrib>Murakami, Satoshi</creatorcontrib><creatorcontrib>Sano, Yukari</creatorcontrib><creatorcontrib>Kimura, Akane</creatorcontrib><creatorcontrib>Sugiyama, Yuuta</creatorcontrib><creatorcontrib>Ando, Akikazu</creatorcontrib><creatorcontrib>Fujii, Takeshi</creatorcontrib><creatorcontrib>Miyashita, Kiyotaka</creatorcontrib><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>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><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saito, Akihiro</au><au>Ebise, Hiroki</au><au>Orihara, Yukari</au><au>Murakami, Satoshi</au><au>Sano, Yukari</au><au>Kimura, Akane</au><au>Sugiyama, Yuuta</au><au>Ando, Akikazu</au><au>Fujii, Takeshi</au><au>Miyashita, Kiyotaka</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2013-03</date><risdate>2013</risdate><volume>340</volume><issue>1</issue><spage>33</spage><epage>40</epage><pages>33-40</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N′-diacetylchitobiose [(GlcNAc)2] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and assimilation of chitin, we obtained and characterized a recombinant DasD protein and a dasD-null mutant of S. coelicolor A3(2). The recombinant DasD protein produced in Escherichia coli showed N-acetyl-β-d-glucosaminidase (GlcNAcase) activity and its optimum temperature and pH were 40 °C and 7, respectively. dasD transcription was strongly induced in the presence of chitin, weakly by chitosan, but not by cellulose or xylan in S. coelicolor A3(2). Immuno-blot analysis demonstrated that DasD is a cytoplasmic protein. The dasD-null mutant exhibited cellular GlcNAcase activity which was comparable with that of the parent strain M145. DasD, thus, did not seem to be a major GlcNAcase. Induced extracellular chitinase activity in the dasD-null mutant was, interestingly, higher than M145, in the presence of colloidal chitin or (GlcNAc)2. In contrast to M145, (GlcNAc)2 temporally accumulated in the culture supernatant of the dasD-null mutant in the presence of colloidal chitin.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>23278377</pmid><doi>10.1111/1574-6968.12069</doi><tpages>8</tpages></addata></record> |
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| ispartof | FEMS microbiology letters, 2013-03, Vol.340 (1), p.33-40 |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Acetylglucosaminidase - genetics Acetylglucosaminidase - metabolism actinomycetes Bacteriology Biological and medical sciences Chitin - metabolism chitinase chitobiase Cloning, Molecular Cytoplasm - enzymology Enzyme Stability Escherichia coli Fundamental and applied biological sciences. Psychology Gene Deletion Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic GH family 3 glycoside hydrolase Hydrogen-Ion Concentration Microbiology Miscellaneous Recombinant Proteins - genetics Recombinant Proteins - metabolism Streptomyces coelicolor Streptomyces coelicolor - enzymology Streptomyces coelicolor - genetics Streptomyces coelicolor - metabolism Temperature |
| title | Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2) |
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