Improved lanthipeptide detection and prediction for antiSMASH.
Lanthipeptides are a class of ribosomally synthesised and post-translationally modified peptide (RiPP) natural products from the bacterial secondary metabolism. Their name is derived from the characteristic lanthionine or methyl-lanthionine residues contained in the processed peptide. Lanthipeptides...
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| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0089420&type=printable |
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| author | Kai Blin Daniyal Kazempour Wolfgang Wohlleben Tilmann Weber |
| author_facet | Kai Blin Daniyal Kazempour Wolfgang Wohlleben Tilmann Weber |
| author_sort | Kai Blin |
| collection | DOAJ |
| description | Lanthipeptides are a class of ribosomally synthesised and post-translationally modified peptide (RiPP) natural products from the bacterial secondary metabolism. Their name is derived from the characteristic lanthionine or methyl-lanthionine residues contained in the processed peptide. Lanthipeptides that possess an antibacterial activity are called lantibiotics. Whereas multiple tools exist to identify lanthipeptide gene clusters from genomic data, no programs are available to predict the post-translational modifications of lanthipeptides, such as the proteolytic cleavage of the leader peptide part or tailoring modifications based on the analysis of the gene cluster sequence. antiSMASH is a software pipeline for the identification of secondary metabolite biosynthetic clusters from genomic input and the prediction of products produced by the identified clusters. Here we present a novel antiSMASH module using a rule-based approach to combine signature motifs for biosynthetic enzymes and lanthipeptide-specific cleavage site motifs to identify lanthipeptide clusters in genomic data, assign the specific lanthipeptide class, predict prepeptide cleavage, tailoring reactions, and the processed molecular weight of the mature peptide products. |
| format | Article |
| id | doaj-art-eaf9dd6b3d8243299c9a46349ed7cc86 |
| institution | DOAJ |
| issn | 1932-6203 |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-eaf9dd6b3d8243299c9a46349ed7cc862025-08-20T03:11:55ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0192e8942010.1371/journal.pone.0089420Improved lanthipeptide detection and prediction for antiSMASH.Kai BlinDaniyal KazempourWolfgang WohllebenTilmann WeberLanthipeptides are a class of ribosomally synthesised and post-translationally modified peptide (RiPP) natural products from the bacterial secondary metabolism. Their name is derived from the characteristic lanthionine or methyl-lanthionine residues contained in the processed peptide. Lanthipeptides that possess an antibacterial activity are called lantibiotics. Whereas multiple tools exist to identify lanthipeptide gene clusters from genomic data, no programs are available to predict the post-translational modifications of lanthipeptides, such as the proteolytic cleavage of the leader peptide part or tailoring modifications based on the analysis of the gene cluster sequence. antiSMASH is a software pipeline for the identification of secondary metabolite biosynthetic clusters from genomic input and the prediction of products produced by the identified clusters. Here we present a novel antiSMASH module using a rule-based approach to combine signature motifs for biosynthetic enzymes and lanthipeptide-specific cleavage site motifs to identify lanthipeptide clusters in genomic data, assign the specific lanthipeptide class, predict prepeptide cleavage, tailoring reactions, and the processed molecular weight of the mature peptide products.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0089420&type=printable |
| spellingShingle | Kai Blin Daniyal Kazempour Wolfgang Wohlleben Tilmann Weber Improved lanthipeptide detection and prediction for antiSMASH. PLoS ONE |
| title | Improved lanthipeptide detection and prediction for antiSMASH. |
| title_full | Improved lanthipeptide detection and prediction for antiSMASH. |
| title_fullStr | Improved lanthipeptide detection and prediction for antiSMASH. |
| title_full_unstemmed | Improved lanthipeptide detection and prediction for antiSMASH. |
| title_short | Improved lanthipeptide detection and prediction for antiSMASH. |
| title_sort | improved lanthipeptide detection and prediction for antismash |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0089420&type=printable |
| work_keys_str_mv | AT kaiblin improvedlanthipeptidedetectionandpredictionforantismash AT daniyalkazempour improvedlanthipeptidedetectionandpredictionforantismash AT wolfgangwohlleben improvedlanthipeptidedetectionandpredictionforantismash AT tilmannweber improvedlanthipeptidedetectionandpredictionforantismash |