Prepeptide sequence of cinnamycin (Ro 09–0198): the first structural gene of a duramycin‐type lantibiotic
The tetracyclic polypeptide antibiotic cinnamycin (Ro 90–0198) belongs to the duramycin‐type lantibiotics and contains the unusual amino acids threo‐3‐methyl‐lanthionine, meso‐lanthionine, lysinoalanine and 3‐hydroxy‐aspartic acid. Its structural gene, referred to as cinA, has been identified on iso...
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| Veröffentlicht in: | European journal of biochemistry 1991-07, Vol.199 (2), p.411-415 |
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| creator | KALETTA, Cortina ENTIAN, Karl‐Dieter JUNG, Günther |
| description | The tetracyclic polypeptide antibiotic cinnamycin (Ro 90–0198) belongs to the duramycin‐type lantibiotics and contains the unusual amino acids threo‐3‐methyl‐lanthionine, meso‐lanthionine, lysinoalanine and 3‐hydroxy‐aspartic acid. Its structural gene, referred to as cinA, has been identified on isolated chromosomal DNA of the Ro 09–0198‐producing strain Streptoverticillium griseoverticillatum via a 39‐residue oligonucleotide probe derived from fragment 7–19 of the hypothetical prolantibiotic sequence CRQSCSFGPFTFVCDGNTK. This propeptide part was then found within an open reading frame of 77 amino acids. In contrast to the nisin‐type prelantibiotics, this first duramycin‐type prelantibiotic has an unusually long leader sequence of 58 amino acids. It also differs in the processing site and the direction of the formation of the threo‐3‐methyl‐lanthionine bridges is from N‐terminal cysteine to C‐terminal dehydrated threonine residues, whereas the meso‐lanthionine and lysinoalanine bridges are formed by addition reactions from C‐terminal cysteine or lysine to N‐terminal dehyrated serine residues. |
| doi_str_mv | 10.1111/j.1432-1033.1991.tb16138.x |
| format | Article |
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Its structural gene, referred to as cinA, has been identified on isolated chromosomal DNA of the Ro 09–0198‐producing strain Streptoverticillium griseoverticillatum via a 39‐residue oligonucleotide probe derived from fragment 7–19 of the hypothetical prolantibiotic sequence CRQSCSFGPFTFVCDGNTK. This propeptide part was then found within an open reading frame of 77 amino acids. In contrast to the nisin‐type prelantibiotics, this first duramycin‐type prelantibiotic has an unusually long leader sequence of 58 amino acids. It also differs in the processing site and the direction of the formation of the threo‐3‐methyl‐lanthionine bridges is from N‐terminal cysteine to C‐terminal dehydrated threonine residues, whereas the meso‐lanthionine and lysinoalanine bridges are formed by addition reactions from C‐terminal cysteine or lysine to N‐terminal dehyrated serine residues.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1991.tb16138.x</identifier><identifier>PMID: 2070795</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Anti-Bacterial Agents - biosynthesis ; Antibiotics (antibacterial agents, antifungal agents) ; Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents ; Applied microbiology ; Bacteriocins ; Base Sequence ; Biological and medical sciences ; DNA, Bacterial - genetics ; DNA, Bacterial - isolation & purification ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; Microbiology ; Molecular Sequence Data ; Oligonucleotide Probes ; Peptides, Cyclic ; Plasmids ; Protein Conformation ; Protein Precursors - genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Streptomycetaceae - genetics</subject><ispartof>European journal of biochemistry, 1991-07, Vol.199 (2), p.411-415</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4961-b55ecc467e74f88a332f281e24c3a76e914b89ba6557704649e947d1d78d92653</citedby><cites>FETCH-LOGICAL-c4961-b55ecc467e74f88a332f281e24c3a76e914b89ba6557704649e947d1d78d92653</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5598941$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2070795$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KALETTA, Cortina</creatorcontrib><creatorcontrib>ENTIAN, Karl‐Dieter</creatorcontrib><creatorcontrib>JUNG, Günther</creatorcontrib><title>Prepeptide sequence of cinnamycin (Ro 09–0198): the first structural gene of a duramycin‐type lantibiotic</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The tetracyclic polypeptide antibiotic cinnamycin (Ro 90–0198) belongs to the duramycin‐type lantibiotics and contains the unusual amino acids threo‐3‐methyl‐lanthionine, meso‐lanthionine, lysinoalanine and 3‐hydroxy‐aspartic acid. Its structural gene, referred to as cinA, has been identified on isolated chromosomal DNA of the Ro 09–0198‐producing strain Streptoverticillium griseoverticillatum via a 39‐residue oligonucleotide probe derived from fragment 7–19 of the hypothetical prolantibiotic sequence CRQSCSFGPFTFVCDGNTK. This propeptide part was then found within an open reading frame of 77 amino acids. In contrast to the nisin‐type prelantibiotics, this first duramycin‐type prelantibiotic has an unusually long leader sequence of 58 amino acids. It also differs in the processing site and the direction of the formation of the threo‐3‐methyl‐lanthionine bridges is from N‐terminal cysteine to C‐terminal dehydrated threonine residues, whereas the meso‐lanthionine and lysinoalanine bridges are formed by addition reactions from C‐terminal cysteine or lysine to N‐terminal dehyrated serine residues.</description><subject>Amino Acid Sequence</subject><subject>Anti-Bacterial Agents - biosynthesis</subject><subject>Antibiotics (antibacterial agents, antifungal agents)</subject><subject>Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents</subject><subject>Applied microbiology</subject><subject>Bacteriocins</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>DNA, Bacterial - genetics</subject><subject>DNA, Bacterial - isolation & purification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Oligonucleotide Probes</subject><subject>Peptides, Cyclic</subject><subject>Plasmids</subject><subject>Protein Conformation</subject><subject>Protein Precursors - genetics</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Streptomycetaceae - genetics</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkdtqFTEUhoModbf6CEIQEb2YMZnJsTeipa2FguLhOmQyazSbOTXJYPddH6HgG_ZJOrt72LfS3CzC__1ZK-tH6DUlOZ3Ph3VOWVlklJRlTrWmeaqooKXKr5-g1V56ilaEUJYVmovn6DDGNSFEaCEP0EFBJJGar1D3LcAIY_I14AhXE_QO8NBg5_vedpu54HffB0z03c0_QrV6f4zTH8CNDzHhmMLk0hRsi39D_-CzuJ7vD8a7m9u0GQG3tk--8kPy7gV61tg2wsulHqFfZ6c_T75kl1_PL04-XWaOaUGzinNwjgkJkjVK2bIsmkJRKJgrrRSgKauUrqzgXErCBNOgmaxpLVWtC8HLI_R29-4YhvlPMZnORwftPAoMUzSKCKmUYP8FqSAFL6SeweMd6MIQY4DGjMF3NmwMJWYbilmb7ebNdvNmG4pZQjHXs_nV0mWqOqj31iWFWX-z6DY62zbB9s7HPca5VprRGfu4w_76FjaPGMCcnX7-wSgt7wHz9anK</recordid><startdate>19910715</startdate><enddate>19910715</enddate><creator>KALETTA, Cortina</creator><creator>ENTIAN, Karl‐Dieter</creator><creator>JUNG, Günther</creator><general>Blackwell Publishing Ltd</general><general>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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19910715</creationdate><title>Prepeptide sequence of cinnamycin (Ro 09–0198): the first structural gene of a duramycin‐type lantibiotic</title><author>KALETTA, Cortina ; ENTIAN, Karl‐Dieter ; JUNG, Günther</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4961-b55ecc467e74f88a332f281e24c3a76e914b89ba6557704649e947d1d78d92653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Anti-Bacterial Agents - biosynthesis</topic><topic>Antibiotics (antibacterial agents, antifungal agents)</topic><topic>Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents</topic><topic>Applied microbiology</topic><topic>Bacteriocins</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>DNA, Bacterial - genetics</topic><topic>DNA, Bacterial - isolation & purification</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Oligonucleotide Probes</topic><topic>Peptides, Cyclic</topic><topic>Plasmids</topic><topic>Protein Conformation</topic><topic>Protein Precursors - genetics</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Streptomycetaceae - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KALETTA, Cortina</creatorcontrib><creatorcontrib>ENTIAN, Karl‐Dieter</creatorcontrib><creatorcontrib>JUNG, Günther</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KALETTA, Cortina</au><au>ENTIAN, Karl‐Dieter</au><au>JUNG, Günther</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prepeptide sequence of cinnamycin (Ro 09–0198): the first structural gene of a duramycin‐type lantibiotic</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1991-07-15</date><risdate>1991</risdate><volume>199</volume><issue>2</issue><spage>411</spage><epage>415</epage><pages>411-415</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The tetracyclic polypeptide antibiotic cinnamycin (Ro 90–0198) belongs to the duramycin‐type lantibiotics and contains the unusual amino acids threo‐3‐methyl‐lanthionine, meso‐lanthionine, lysinoalanine and 3‐hydroxy‐aspartic acid. Its structural gene, referred to as cinA, has been identified on isolated chromosomal DNA of the Ro 09–0198‐producing strain Streptoverticillium griseoverticillatum via a 39‐residue oligonucleotide probe derived from fragment 7–19 of the hypothetical prolantibiotic sequence CRQSCSFGPFTFVCDGNTK. This propeptide part was then found within an open reading frame of 77 amino acids. In contrast to the nisin‐type prelantibiotics, this first duramycin‐type prelantibiotic has an unusually long leader sequence of 58 amino acids. It also differs in the processing site and the direction of the formation of the threo‐3‐methyl‐lanthionine bridges is from N‐terminal cysteine to C‐terminal dehydrated threonine residues, whereas the meso‐lanthionine and lysinoalanine bridges are formed by addition reactions from C‐terminal cysteine or lysine to N‐terminal dehyrated serine residues.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2070795</pmid><doi>10.1111/j.1432-1033.1991.tb16138.x</doi><tpages>5</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 1991-07, Vol.199 (2), p.411-415 |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Anti-Bacterial Agents - biosynthesis Antibiotics (antibacterial agents, antifungal agents) Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents Applied microbiology Bacteriocins Base Sequence Biological and medical sciences DNA, Bacterial - genetics DNA, Bacterial - isolation & purification Fundamental and applied biological sciences. Psychology Genes, Bacterial Microbiology Molecular Sequence Data Oligonucleotide Probes Peptides, Cyclic Plasmids Protein Conformation Protein Precursors - genetics Restriction Mapping Sequence Homology, Nucleic Acid Streptomycetaceae - genetics |
| title | Prepeptide sequence of cinnamycin (Ro 09–0198): the first structural gene of a duramycin‐type lantibiotic |
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