The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis
Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The transl...
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| Format: | Article |
| Language: | English |
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The American Phytopathological Society
2001-03-01
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| Series: | Molecular Plant-Microbe Interactions |
| Subjects: | |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI.2001.14.3.336 |
| _version_ | 1818757446121816064 |
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| author | Brenda K. Scholz-Schroeder Michael L. Hutchison Ingeborg Grgurina Dennis C. Gross |
| author_facet | Brenda K. Scholz-Schroeder Michael L. Hutchison Ingeborg Grgurina Dennis C. Gross |
| author_sort | Brenda K. Scholz-Schroeder |
| collection | DOAJ |
| description | Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The translated protein sequence encompasses a complete amino acid activation module containing the conserved domains characteristic of peptide synthetases. Analysis of the substrate specificity region of this module indicates that it incorporates 2,3-dehydroaminobutyric acid into the syringopeptin peptide structure. Bioassay and high performance liquid chromatography data confirmed that disruption of the sypA gene in strain B301D resulted in the loss of syringopeptin production. The contribution of syringopeptin and syringomycin to the virulence of P. syringae pv. syringae strain B301D was examined in immature sweet cherry with sypA and syrB1 synthetase mutants defective in the production of the two toxins, respectively. Syringopeptin (sypA) and syringomycin (syrB1) mutants were reduced in virulence 59 and 26%, respectively, compared with the parental strain in cherry, whereas the syringopeptin-syringomycin double mutant was reduced 76% in virulence. These data demonstrate that syringopeptin and syringomycin are major virulence determinants of P. syringae pv. syringae. |
| first_indexed | 2024-12-18T06:11:04Z |
| format | Article |
| id | doaj.art-a0d7f672fd724d779afc56d6a2f7757c |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-12-18T06:11:04Z |
| publishDate | 2001-03-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-a0d7f672fd724d779afc56d6a2f7757c2022-12-21T21:18:24ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062001-03-0114333634810.1094/MPMI.2001.14.3.336The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant AnalysisBrenda K. Scholz-SchroederMichael L. HutchisonIngeborg GrgurinaDennis C. GrossSequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The translated protein sequence encompasses a complete amino acid activation module containing the conserved domains characteristic of peptide synthetases. Analysis of the substrate specificity region of this module indicates that it incorporates 2,3-dehydroaminobutyric acid into the syringopeptin peptide structure. Bioassay and high performance liquid chromatography data confirmed that disruption of the sypA gene in strain B301D resulted in the loss of syringopeptin production. The contribution of syringopeptin and syringomycin to the virulence of P. syringae pv. syringae strain B301D was examined in immature sweet cherry with sypA and syrB1 synthetase mutants defective in the production of the two toxins, respectively. Syringopeptin (sypA) and syringomycin (syrB1) mutants were reduced in virulence 59 and 26%, respectively, compared with the parental strain in cherry, whereas the syringopeptin-syringomycin double mutant was reduced 76% in virulence. These data demonstrate that syringopeptin and syringomycin are major virulence determinants of P. syringae pv. syringae.https://apsjournals.apsnet.org/doi/10.1094/MPMI.2001.14.3.336lipopeptide toxinnecrosis-inducing toxinnonribosomal peptide synthetasephytotoxin |
| spellingShingle | Brenda K. Scholz-Schroeder Michael L. Hutchison Ingeborg Grgurina Dennis C. Gross The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis Molecular Plant-Microbe Interactions lipopeptide toxin necrosis-inducing toxin nonribosomal peptide synthetase phytotoxin |
| title | The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis |
| title_full | The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis |
| title_fullStr | The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis |
| title_full_unstemmed | The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis |
| title_short | The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis |
| title_sort | contribution of syringopeptin and syringomycin to virulence of pseudomonas syringae pv syringae strain b301d on the basis of sypa and syrb1 biosynthesis mutant analysis |
| topic | lipopeptide toxin necrosis-inducing toxin nonribosomal peptide synthetase phytotoxin |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI.2001.14.3.336 |
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