Mutational and comparative analysis of streptolysin O, an oxygen-labile streptococcal hemolysin
The structural gene of streptolysin O was cloned from Streptococcus pyogenes strain Sa and S. equisimilis H46A, and the nucleotide sequences were compared with those of strain Richards. To obtain the minimal active fragment of the toxin and to elucidate structure-function relationships in hemolytic...
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2001-12, Vol.65 (12), p.2682-2689 |
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description | The structural gene of streptolysin O was cloned from Streptococcus pyogenes strain Sa and S. equisimilis H46A, and the nucleotide sequences were compared with those of strain Richards. To obtain the minimal active fragment of the toxin and to elucidate structure-function relationships in hemolytic function, streptolysin O mutants deleted in N- and C-terminal regions were constructed. Internal amino acid residues were also replaced by introduction of point mutations. Analyses of these mutants showed that considerable activity was retained even after deletion of the N-terminal 107 residues, but genetic removal of the ultimate C-terminal residue resulted in a marked decrease in hemolytic function. By removal in succession, hemolytic activity declined exponentially, and only 0.002% of the activity remained after deletion of the C-terminal four residues. Nucleotide replacement experiments indicated pivotal roles of I202, V217, D324-L325, V339, and H469 residues in hemolysis. |
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(Fukui Medical School, Matsuoka (Japan)) ; Kimoto, H ; Taketo, Y ; Taketo, A</creator><creatorcontrib>Yamamoto, I. (Fukui Medical School, Matsuoka (Japan)) ; Kimoto, H ; Taketo, Y ; Taketo, A</creatorcontrib><description>The structural gene of streptolysin O was cloned from Streptococcus pyogenes strain Sa and S. equisimilis H46A, and the nucleotide sequences were compared with those of strain Richards. To obtain the minimal active fragment of the toxin and to elucidate structure-function relationships in hemolytic function, streptolysin O mutants deleted in N- and C-terminal regions were constructed. Internal amino acid residues were also replaced by introduction of point mutations. Analyses of these mutants showed that considerable activity was retained even after deletion of the N-terminal 107 residues, but genetic removal of the ultimate C-terminal residue resulted in a marked decrease in hemolytic function. By removal in succession, hemolytic activity declined exponentially, and only 0.002% of the activity remained after deletion of the C-terminal four residues. Nucleotide replacement experiments indicated pivotal roles of I202, V217, D324-L325, V339, and H469 residues in hemolysis.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.65.2682</identifier><identifier>PMID: 11826964</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological and medical sciences ; Biotechnology ; DNA Primers ; Fundamental and applied biological sciences. Psychology ; GENES ; Genes, Bacterial ; HAEMOLYSIS ; hemolysin ; Hemolysin Proteins - metabolism ; MOLECULAR CLONING ; Molecular Sequence Data ; MUTATION ; mutational analysis ; NUCLEOTIDE SEQUENCE ; Oxygen - metabolism ; Plasmids ; Point Mutation ; Sheep ; STREPTOCOCCUS ; Streptococcus pyogenes - genetics ; Streptococcus pyogenes - metabolism ; streptolysin O ; Streptolysins - chemistry ; Streptolysins - genetics ; Streptolysins - metabolism</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2001-12, Vol.65 (12), p.2682-2689</ispartof><rights>2001 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2001</rights><rights>2002 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c696t-63c5d5339c2e7b5156738c0985b7b209eb7e9c2d68160d9d3284bb23f1d0fe893</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13464279$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11826964$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamamoto, I. (Fukui Medical School, Matsuoka (Japan))</creatorcontrib><creatorcontrib>Kimoto, H</creatorcontrib><creatorcontrib>Taketo, Y</creatorcontrib><creatorcontrib>Taketo, A</creatorcontrib><title>Mutational and comparative analysis of streptolysin O, an oxygen-labile streptococcal hemolysin</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The structural gene of streptolysin O was cloned from Streptococcus pyogenes strain Sa and S. equisimilis H46A, and the nucleotide sequences were compared with those of strain Richards. To obtain the minimal active fragment of the toxin and to elucidate structure-function relationships in hemolytic function, streptolysin O mutants deleted in N- and C-terminal regions were constructed. Internal amino acid residues were also replaced by introduction of point mutations. Analyses of these mutants showed that considerable activity was retained even after deletion of the N-terminal 107 residues, but genetic removal of the ultimate C-terminal residue resulted in a marked decrease in hemolytic function. By removal in succession, hemolytic activity declined exponentially, and only 0.002% of the activity remained after deletion of the C-terminal four residues. Nucleotide replacement experiments indicated pivotal roles of I202, V217, D324-L325, V339, and H469 residues in hemolysis.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacterial Proteins</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>DNA Primers</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENES</subject><subject>Genes, Bacterial</subject><subject>HAEMOLYSIS</subject><subject>hemolysin</subject><subject>Hemolysin Proteins - metabolism</subject><subject>MOLECULAR CLONING</subject><subject>Molecular Sequence Data</subject><subject>MUTATION</subject><subject>mutational analysis</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>Oxygen - metabolism</subject><subject>Plasmids</subject><subject>Point Mutation</subject><subject>Sheep</subject><subject>STREPTOCOCCUS</subject><subject>Streptococcus pyogenes - genetics</subject><subject>Streptococcus pyogenes - metabolism</subject><subject>streptolysin O</subject><subject>Streptolysins - chemistry</subject><subject>Streptolysins - genetics</subject><subject>Streptolysins - metabolism</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcuLFDEQxoMo7uzqybPSIOtFe8z7cZTFJyvrQc8hSafXXtKdMelW57-3hp5lQQQhEKrqVx9V9SH0hOAtoYq89t5vpdhSqek9tCGMq1Yaru6jDTZEtpoLcoJOa73BGBKCPEQnhGgqjeQbZD8vs5uHPLnUuKlrQh53rkDmZ4TYpX0dapP7ps4l7uZ8iKfm6hXUmvx7fx2nNjk_pHgLhBwCSH2P48o-Qg96l2p8fPzP0Ld3b79efGgvr95_vHhz2QaYY24lC6ITjJlAo_KCCKmYDtho4ZWn2ESvItQ6qYnEnekY1dx7ynrS4T5qw87Qi1V3V_KPJdbZjkMNMSU3xbxUqyinRAn8X5BoLrVmAsDnf4E3eSlwEmA4N5xJQRVQL1cqlFxrib3dlWF0ZW8Jtgd7LNhjpbAHe4B-dtRc_Bi7O_boBwDnR8BVuGNf3BSGescxLjlVh3Xlyg1Tn8vofuWSOju7fcrlton9e4Kna2PvsnXXBbhPXyjG8JiEff4A9Suy6g</recordid><startdate>20011201</startdate><enddate>20011201</enddate><creator>Yamamoto, I. (Fukui Medical School, Matsuoka (Japan))</creator><creator>Kimoto, H</creator><creator>Taketo, Y</creator><creator>Taketo, A</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20011201</creationdate><title>Mutational and comparative analysis of streptolysin O, an oxygen-labile streptococcal hemolysin</title><author>Yamamoto, I. (Fukui Medical School, Matsuoka (Japan)) ; Kimoto, H ; Taketo, Y ; Taketo, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c696t-63c5d5339c2e7b5156738c0985b7b209eb7e9c2d68160d9d3284bb23f1d0fe893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacterial Proteins</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>DNA Primers</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENES</topic><topic>Genes, Bacterial</topic><topic>HAEMOLYSIS</topic><topic>hemolysin</topic><topic>Hemolysin Proteins - metabolism</topic><topic>MOLECULAR CLONING</topic><topic>Molecular Sequence Data</topic><topic>MUTATION</topic><topic>mutational analysis</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>Oxygen - metabolism</topic><topic>Plasmids</topic><topic>Point Mutation</topic><topic>Sheep</topic><topic>STREPTOCOCCUS</topic><topic>Streptococcus pyogenes - genetics</topic><topic>Streptococcus pyogenes - metabolism</topic><topic>streptolysin O</topic><topic>Streptolysins - chemistry</topic><topic>Streptolysins - genetics</topic><topic>Streptolysins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamamoto, I. (Fukui Medical School, Matsuoka (Japan))</creatorcontrib><creatorcontrib>Kimoto, H</creatorcontrib><creatorcontrib>Taketo, Y</creatorcontrib><creatorcontrib>Taketo, A</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamamoto, I. (Fukui Medical School, Matsuoka (Japan))</au><au>Kimoto, H</au><au>Taketo, Y</au><au>Taketo, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutational and comparative analysis of streptolysin O, an oxygen-labile streptococcal hemolysin</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2001-12-01</date><risdate>2001</risdate><volume>65</volume><issue>12</issue><spage>2682</spage><epage>2689</epage><pages>2682-2689</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>The structural gene of streptolysin O was cloned from Streptococcus pyogenes strain Sa and S. equisimilis H46A, and the nucleotide sequences were compared with those of strain Richards. To obtain the minimal active fragment of the toxin and to elucidate structure-function relationships in hemolytic function, streptolysin O mutants deleted in N- and C-terminal regions were constructed. Internal amino acid residues were also replaced by introduction of point mutations. Analyses of these mutants showed that considerable activity was retained even after deletion of the N-terminal 107 residues, but genetic removal of the ultimate C-terminal residue resulted in a marked decrease in hemolytic function. By removal in succession, hemolytic activity declined exponentially, and only 0.002% of the activity remained after deletion of the C-terminal four residues. Nucleotide replacement experiments indicated pivotal roles of I202, V217, D324-L325, V339, and H469 residues in hemolysis.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>11826964</pmid><doi>10.1271/bbb.65.2682</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
subjects | Amino Acid Sequence Animals Bacterial Proteins Base Sequence Biological and medical sciences Biotechnology DNA Primers Fundamental and applied biological sciences. Psychology GENES Genes, Bacterial HAEMOLYSIS hemolysin Hemolysin Proteins - metabolism MOLECULAR CLONING Molecular Sequence Data MUTATION mutational analysis NUCLEOTIDE SEQUENCE Oxygen - metabolism Plasmids Point Mutation Sheep STREPTOCOCCUS Streptococcus pyogenes - genetics Streptococcus pyogenes - metabolism streptolysin O Streptolysins - chemistry Streptolysins - genetics Streptolysins - metabolism |
title | Mutational and comparative analysis of streptolysin O, an oxygen-labile streptococcal hemolysin |
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