Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production
<p>Abstract</p> <p>Background</p> <p>Mangotoxin is an antimetabolite toxin that is produced by strains of <it>Pseudomonas syringae </it>pv. <it>syringae</it>; mangotoxin-producing strains are primarily isolated from mango tissues with symptoms of...
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| Language: | English |
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BMC
2012-01-01
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| Series: | BMC Microbiology |
| Online Access: | http://www.biomedcentral.com/1471-2180/12/10 |
| _version_ | 1818143615260557312 |
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| author | Arrebola Eva Carrión Víctor J Cazorla Francisco M Pérez-García Alejandro Murillo Jesús de Vicente Antonio |
| author_facet | Arrebola Eva Carrión Víctor J Cazorla Francisco M Pérez-García Alejandro Murillo Jesús de Vicente Antonio |
| author_sort | Arrebola Eva |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Mangotoxin is an antimetabolite toxin that is produced by strains of <it>Pseudomonas syringae </it>pv. <it>syringae</it>; mangotoxin-producing strains are primarily isolated from mango tissues with symptoms of bacterial apical necrosis. The toxin is an oligopeptide that inhibits ornithine N-acetyl transferase (OAT), a key enzyme in the biosynthetic pathway of the essential amino acids ornithine and arginine. The involvement of a putative nonribosomal peptide synthetase gene (<it>mgo</it>A) in mangotoxin production and virulence has been reported.</p> <p>Results</p> <p>In the present study, we performed a RT-PCR analysis, insertional inactivation mutagenesis, a promoter expression analysis and terminator localisation to study the gene cluster containing the <it>mgo</it>A gene. Additionally, we evaluated the importance of <it>mgo</it>C, <it>mgo</it>A and <it>mgo</it>D in mangotoxin production. A sequence analysis revealed an operon-like organisation. A promoter sequence was located upstream of the <it>mgo</it>B gene and was found to drive <it>lac</it>Z transcription. Two terminators were located downstream of the <it>mgo</it>D gene. RT-PCR experiments indicated that the four genes (<it>mgo</it>BCAD) constitute a transcriptional unit. This operon is similar in genetic organisation to those in the three other <it>P. syringae </it>pathovars for which complete genomes are available (<it>P. syringae </it>pv. <it>syringae </it>B728a, <it>P. syringae </it>pv. <it>tomato </it>DC3000 and <it>P. syringae </it>pv. <it>phaseolicola </it>1448A). Interestingly, none of these three reference strains is capable of producing mangotoxin. Additionally, extract complementation resulted in a recovery of mangotoxin production when the defective mutant was complemented with wild-type extracts.</p> <p>Conclusions</p> <p>The results of this study confirm that <it>mgo</it>B, <it>mgo</it>C, <it>mgo</it>A and <it>mgo</it>D function as a transcriptional unit and operon. While this operon is composed of four genes, only the last three are directly involved in mangotoxin production.</p> |
| first_indexed | 2024-12-11T11:34:29Z |
| format | Article |
| id | doaj.art-c26b59f546364a8f87b84c93db3b8f49 |
| institution | Directory Open Access Journal |
| issn | 1471-2180 |
| language | English |
| last_indexed | 2024-12-11T11:34:29Z |
| publishDate | 2012-01-01 |
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| spelling | doaj.art-c26b59f546364a8f87b84c93db3b8f492022-12-22T01:08:48ZengBMCBMC Microbiology1471-21802012-01-011211010.1186/1471-2180-12-10Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin productionArrebola EvaCarrión Víctor JCazorla Francisco MPérez-García AlejandroMurillo Jesúsde Vicente Antonio<p>Abstract</p> <p>Background</p> <p>Mangotoxin is an antimetabolite toxin that is produced by strains of <it>Pseudomonas syringae </it>pv. <it>syringae</it>; mangotoxin-producing strains are primarily isolated from mango tissues with symptoms of bacterial apical necrosis. The toxin is an oligopeptide that inhibits ornithine N-acetyl transferase (OAT), a key enzyme in the biosynthetic pathway of the essential amino acids ornithine and arginine. The involvement of a putative nonribosomal peptide synthetase gene (<it>mgo</it>A) in mangotoxin production and virulence has been reported.</p> <p>Results</p> <p>In the present study, we performed a RT-PCR analysis, insertional inactivation mutagenesis, a promoter expression analysis and terminator localisation to study the gene cluster containing the <it>mgo</it>A gene. Additionally, we evaluated the importance of <it>mgo</it>C, <it>mgo</it>A and <it>mgo</it>D in mangotoxin production. A sequence analysis revealed an operon-like organisation. A promoter sequence was located upstream of the <it>mgo</it>B gene and was found to drive <it>lac</it>Z transcription. Two terminators were located downstream of the <it>mgo</it>D gene. RT-PCR experiments indicated that the four genes (<it>mgo</it>BCAD) constitute a transcriptional unit. This operon is similar in genetic organisation to those in the three other <it>P. syringae </it>pathovars for which complete genomes are available (<it>P. syringae </it>pv. <it>syringae </it>B728a, <it>P. syringae </it>pv. <it>tomato </it>DC3000 and <it>P. syringae </it>pv. <it>phaseolicola </it>1448A). Interestingly, none of these three reference strains is capable of producing mangotoxin. Additionally, extract complementation resulted in a recovery of mangotoxin production when the defective mutant was complemented with wild-type extracts.</p> <p>Conclusions</p> <p>The results of this study confirm that <it>mgo</it>B, <it>mgo</it>C, <it>mgo</it>A and <it>mgo</it>D function as a transcriptional unit and operon. While this operon is composed of four genes, only the last three are directly involved in mangotoxin production.</p>http://www.biomedcentral.com/1471-2180/12/10 |
| spellingShingle | Arrebola Eva Carrión Víctor J Cazorla Francisco M Pérez-García Alejandro Murillo Jesús de Vicente Antonio Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production BMC Microbiology |
| title | Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production |
| title_full | Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production |
| title_fullStr | Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production |
| title_full_unstemmed | Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production |
| title_short | Characterisation of the <it>mgo </it>operon in <it>Pseudomonas syringae </it>pv. <it>syringae </it>UMAF0158 that is required for mangotoxin production |
| title_sort | characterisation of the it mgo it operon in it pseudomonas syringae it pv it syringae it umaf0158 that is required for mangotoxin production |
| url | http://www.biomedcentral.com/1471-2180/12/10 |
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