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Check the list of papers from NScTI Citrus
Use the filters at the top of the list to select articles by year or by researcher. In the box for each article, use the links ("Summary", "Links", "BibTeX") to open additional information.
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2019
Silva, Caio Cesar Lima; Shimo, Hugo Massayoshi; Felício, Rafael; Mercaldi, Gustavo Fernando; Rocco, Silvana Aparecida; Benedetti, Celso Eduardo
Structure-function relationship of a citrus salicylate methylesterase and role of salicylic acid in citrus canker resistance Journal Article
In: Scientific Reports 2019 9:1, vol. 9, iss. 1, pp. 1-12, 2019, ISSN: 2045-2322.
Abstract | Links | BibTeX | Tags: Biotic, Plant hormones
@article{nokey,
title = {Structure-function relationship of a citrus salicylate methylesterase and role of salicylic acid in citrus canker resistance},
author = {Caio Cesar Lima Silva and Hugo Massayoshi Shimo and Rafael Felício and Gustavo Fernando Mercaldi and Silvana Aparecida Rocco and Celso Eduardo Benedetti},
url = {https://www.nature.com/articles/s41598-019-40552-3},
doi = {10.1038/s41598-019-40552-3},
issn = {2045-2322},
year = {2019},
date = {2019-01-01},
journal = {Scientific Reports 2019 9:1},
volume = {9},
issue = {1},
pages = {1-12},
publisher = {Nature Publishing Group},
abstract = {Salicylic acid (SA) and its methyl ester, methyl salicylate (MeSA) are well known inducers of local and systemic plant defense responses, respectively. MeSA is a major mediator of systemic acquired resistance (SAR) and its conversion back into SA is thought to be required for SAR. In many plant species, conversion of MeSA into SA is mediated by MeSA esterases of the SABP2 family. Here we show that the Citrus sinensis SABP2 homologue protein CsMES1 catalyzes the hydrolysis of MeSA into SA. Molecular modeling studies suggest that CsMES1 shares the same structure and SA-binding mode with tobacco SABP2. However, an amino acid polymorphism in the active site of CsMES1-related proteins suggested an important role in enzyme regulation. We present evidence that the side chain of this polymorphic residue directly influences enzyme activity and SA binding affinity in CsMES proteins. We also show that SA and CsMES1 transcripts preferentially accumulate during the incompatible interaction between Xanthomonas aurantifolii pathotype C and sweet orange plants. Moreover, we demonstrate that SA and MeSA inhibited citrus canker caused by Xanthomonas citri, whereas an inhibitor of CsMES1 enhanced canker formation, suggesting that CsMES1 and SA play a role in the local defense against citrus canker bacteria.},
keywords = {Biotic, Plant hormones},
pubstate = {published},
tppubtype = {article}
}
Salicylic acid (SA) and its methyl ester, methyl salicylate (MeSA) are well known inducers of local and systemic plant defense responses, respectively. MeSA is a major mediator of systemic acquired resistance (SAR) and its conversion back into SA is thought to be required for SAR. In many plant species, conversion of MeSA into SA is mediated by MeSA esterases of the SABP2 family. Here we show that the Citrus sinensis SABP2 homologue protein CsMES1 catalyzes the hydrolysis of MeSA into SA. Molecular modeling studies suggest that CsMES1 shares the same structure and SA-binding mode with tobacco SABP2. However, an amino acid polymorphism in the active site of CsMES1-related proteins suggested an important role in enzyme regulation. We present evidence that the side chain of this polymorphic residue directly influences enzyme activity and SA binding affinity in CsMES proteins. We also show that SA and CsMES1 transcripts preferentially accumulate during the incompatible interaction between Xanthomonas aurantifolii pathotype C and sweet orange plants. Moreover, we demonstrate that SA and MeSA inhibited citrus canker caused by Xanthomonas citri, whereas an inhibitor of CsMES1 enhanced canker formation, suggesting that CsMES1 and SA play a role in the local defense against citrus canker bacteria.
Silva, Caio Cesar Lima; Shimo, Hugo Massayoshi; Felício, Rafael; Mercaldi, Gustavo Fernando; Rocco, Silvana Aparecida; Benedetti, Celso Eduardo
Structure-function relationship of a citrus salicylate methylesterase and role of salicylic acid in citrus canker resistance Journal Article
In: Scientific Reports 2019 9:1, vol. 9, iss. 1, pp. 1-12, 2019, ISSN: 2045-2322.
Abstract | Links | BibTeX | Tags: Biotic, Plant hormones
@article{nokey,
title = {Structure-function relationship of a citrus salicylate methylesterase and role of salicylic acid in citrus canker resistance},
author = {Caio Cesar Lima Silva and Hugo Massayoshi Shimo and Rafael Felício and Gustavo Fernando Mercaldi and Silvana Aparecida Rocco and Celso Eduardo Benedetti},
url = {https://www.nature.com/articles/s41598-019-40552-3},
doi = {10.1038/s41598-019-40552-3},
issn = {2045-2322},
year = {2019},
date = {2019-01-01},
journal = {Scientific Reports 2019 9:1},
volume = {9},
issue = {1},
pages = {1-12},
publisher = {Nature Publishing Group},
abstract = {Salicylic acid (SA) and its methyl ester, methyl salicylate (MeSA) are well known inducers of local and systemic plant defense responses, respectively. MeSA is a major mediator of systemic acquired resistance (SAR) and its conversion back into SA is thought to be required for SAR. In many plant species, conversion of MeSA into SA is mediated by MeSA esterases of the SABP2 family. Here we show that the Citrus sinensis SABP2 homologue protein CsMES1 catalyzes the hydrolysis of MeSA into SA. Molecular modeling studies suggest that CsMES1 shares the same structure and SA-binding mode with tobacco SABP2. However, an amino acid polymorphism in the active site of CsMES1-related proteins suggested an important role in enzyme regulation. We present evidence that the side chain of this polymorphic residue directly influences enzyme activity and SA binding affinity in CsMES proteins. We also show that SA and CsMES1 transcripts preferentially accumulate during the incompatible interaction between Xanthomonas aurantifolii pathotype C and sweet orange plants. Moreover, we demonstrate that SA and MeSA inhibited citrus canker caused by Xanthomonas citri, whereas an inhibitor of CsMES1 enhanced canker formation, suggesting that CsMES1 and SA play a role in the local defense against citrus canker bacteria.},
keywords = {Biotic, Plant hormones},
pubstate = {published},
tppubtype = {article}
}
Salicylic acid (SA) and its methyl ester, methyl salicylate (MeSA) are well known inducers of local and systemic plant defense responses, respectively. MeSA is a major mediator of systemic acquired resistance (SAR) and its conversion back into SA is thought to be required for SAR. In many plant species, conversion of MeSA into SA is mediated by MeSA esterases of the SABP2 family. Here we show that the Citrus sinensis SABP2 homologue protein CsMES1 catalyzes the hydrolysis of MeSA into SA. Molecular modeling studies suggest that CsMES1 shares the same structure and SA-binding mode with tobacco SABP2. However, an amino acid polymorphism in the active site of CsMES1-related proteins suggested an important role in enzyme regulation. We present evidence that the side chain of this polymorphic residue directly influences enzyme activity and SA binding affinity in CsMES proteins. We also show that SA and CsMES1 transcripts preferentially accumulate during the incompatible interaction between Xanthomonas aurantifolii pathotype C and sweet orange plants. Moreover, we demonstrate that SA and MeSA inhibited citrus canker caused by Xanthomonas citri, whereas an inhibitor of CsMES1 enhanced canker formation, suggesting that CsMES1 and SA play a role in the local defense against citrus canker bacteria.
2018
Lira, Nayara Patricia Vieira De; Pauletti, Bianca Alves; Marques, Ana Carolina; Perez, Carlos Alberto; Caserta, Raquel; Souza, Alessandra Alves De; Vercesi, Aníbal Eugênio; Leme, Adriana Franco Paes; Benedetti, Celso Eduardo
BigR is a sulfide sensor that regulates a sulfur transferase/dioxygenase required for aerobic respiration of plant bacteria under sulfide stress Journal Article
In: Scientific Reports 2018 8:1, vol. 8, iss. 1, pp. 1-13, 2018, ISSN: 2045-2322.
Abstract | Links | BibTeX | Tags: Biotic, Pathogens
@article{nokey,
title = {BigR is a sulfide sensor that regulates a sulfur transferase/dioxygenase required for aerobic respiration of plant bacteria under sulfide stress},
author = {Nayara Patricia Vieira De Lira and Bianca Alves Pauletti and Ana Carolina Marques and Carlos Alberto Perez and Raquel Caserta and Alessandra Alves De Souza and Aníbal Eugênio Vercesi and Adriana Franco Paes Leme and Celso Eduardo Benedetti},
url = {https://www.nature.com/articles/s41598-018-21974-x},
doi = {10.1038/s41598-018-21974-x},
issn = {2045-2322},
year = {2018},
date = {2018-01-01},
journal = {Scientific Reports 2018 8:1},
volume = {8},
issue = {1},
pages = {1-13},
publisher = {Nature Publishing Group},
abstract = {To cope with toxic levels of H2S, the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens employ the bigR operon to oxidize H2S into sulfite. The bigR operon is regulated by the transcriptional repressor BigR and it encodes a bifunctional sulfur transferase (ST) and sulfur dioxygenase (SDO) enzyme, Blh, required for H2S oxidation and bacterial growth under hypoxia. However, how Blh operates to enhance bacterial survival under hypoxia and how BigR is deactivated to derepress operon transcription is unknown. Here, we show that the ST and SDO activities of Blh are in vitro coupled and necessary to oxidize sulfide into sulfite, and that Blh is critical to maintain the oxygen flux during A. tumefaciens respiration when oxygen becomes limited to cells. We also show that H2S and polysulfides inactivate BigR leading to operon transcription. Moreover, we show that sulfite, which is produced by Blh in the ST and SDO reactions, is toxic to Citrus sinensis and that X. fastidiosa-infected plants accumulate sulfite and higher transcript levels of sulfite detoxification enzymes, suggesting that they are under sulfite stress. These results indicate that BigR acts as a sulfide sensor in the H2S oxidation mechanism that allows pathogens to colonize plant tissues where oxygen is a limiting factor.},
keywords = {Biotic, Pathogens},
pubstate = {published},
tppubtype = {article}
}
To cope with toxic levels of H2S, the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens employ the bigR operon to oxidize H2S into sulfite. The bigR operon is regulated by the transcriptional repressor BigR and it encodes a bifunctional sulfur transferase (ST) and sulfur dioxygenase (SDO) enzyme, Blh, required for H2S oxidation and bacterial growth under hypoxia. However, how Blh operates to enhance bacterial survival under hypoxia and how BigR is deactivated to derepress operon transcription is unknown. Here, we show that the ST and SDO activities of Blh are in vitro coupled and necessary to oxidize sulfide into sulfite, and that Blh is critical to maintain the oxygen flux during A. tumefaciens respiration when oxygen becomes limited to cells. We also show that H2S and polysulfides inactivate BigR leading to operon transcription. Moreover, we show that sulfite, which is produced by Blh in the ST and SDO reactions, is toxic to Citrus sinensis and that X. fastidiosa-infected plants accumulate sulfite and higher transcript levels of sulfite detoxification enzymes, suggesting that they are under sulfite stress. These results indicate that BigR acts as a sulfide sensor in the H2S oxidation mechanism that allows pathogens to colonize plant tissues where oxygen is a limiting factor.
Lira, Nayara Patricia Vieira De; Pauletti, Bianca Alves; Marques, Ana Carolina; Perez, Carlos Alberto; Caserta, Raquel; Souza, Alessandra Alves De; Vercesi, Aníbal Eugênio; Leme, Adriana Franco Paes; Benedetti, Celso Eduardo
BigR is a sulfide sensor that regulates a sulfur transferase/dioxygenase required for aerobic respiration of plant bacteria under sulfide stress Journal Article
In: Scientific Reports 2018 8:1, vol. 8, iss. 1, pp. 1-13, 2018, ISSN: 2045-2322.
Abstract | Links | BibTeX | Tags: Biotic, Pathogens
@article{nokey,
title = {BigR is a sulfide sensor that regulates a sulfur transferase/dioxygenase required for aerobic respiration of plant bacteria under sulfide stress},
author = {Nayara Patricia Vieira De Lira and Bianca Alves Pauletti and Ana Carolina Marques and Carlos Alberto Perez and Raquel Caserta and Alessandra Alves De Souza and Aníbal Eugênio Vercesi and Adriana Franco Paes Leme and Celso Eduardo Benedetti},
url = {https://www.nature.com/articles/s41598-018-21974-x},
doi = {10.1038/s41598-018-21974-x},
issn = {2045-2322},
year = {2018},
date = {2018-01-01},
journal = {Scientific Reports 2018 8:1},
volume = {8},
issue = {1},
pages = {1-13},
publisher = {Nature Publishing Group},
abstract = {To cope with toxic levels of H2S, the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens employ the bigR operon to oxidize H2S into sulfite. The bigR operon is regulated by the transcriptional repressor BigR and it encodes a bifunctional sulfur transferase (ST) and sulfur dioxygenase (SDO) enzyme, Blh, required for H2S oxidation and bacterial growth under hypoxia. However, how Blh operates to enhance bacterial survival under hypoxia and how BigR is deactivated to derepress operon transcription is unknown. Here, we show that the ST and SDO activities of Blh are in vitro coupled and necessary to oxidize sulfide into sulfite, and that Blh is critical to maintain the oxygen flux during A. tumefaciens respiration when oxygen becomes limited to cells. We also show that H2S and polysulfides inactivate BigR leading to operon transcription. Moreover, we show that sulfite, which is produced by Blh in the ST and SDO reactions, is toxic to Citrus sinensis and that X. fastidiosa-infected plants accumulate sulfite and higher transcript levels of sulfite detoxification enzymes, suggesting that they are under sulfite stress. These results indicate that BigR acts as a sulfide sensor in the H2S oxidation mechanism that allows pathogens to colonize plant tissues where oxygen is a limiting factor.},
keywords = {Biotic, Pathogens},
pubstate = {published},
tppubtype = {article}
}
To cope with toxic levels of H2S, the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens employ the bigR operon to oxidize H2S into sulfite. The bigR operon is regulated by the transcriptional repressor BigR and it encodes a bifunctional sulfur transferase (ST) and sulfur dioxygenase (SDO) enzyme, Blh, required for H2S oxidation and bacterial growth under hypoxia. However, how Blh operates to enhance bacterial survival under hypoxia and how BigR is deactivated to derepress operon transcription is unknown. Here, we show that the ST and SDO activities of Blh are in vitro coupled and necessary to oxidize sulfide into sulfite, and that Blh is critical to maintain the oxygen flux during A. tumefaciens respiration when oxygen becomes limited to cells. We also show that H2S and polysulfides inactivate BigR leading to operon transcription. Moreover, we show that sulfite, which is produced by Blh in the ST and SDO reactions, is toxic to Citrus sinensis and that X. fastidiosa-infected plants accumulate sulfite and higher transcript levels of sulfite detoxification enzymes, suggesting that they are under sulfite stress. These results indicate that BigR acts as a sulfide sensor in the H2S oxidation mechanism that allows pathogens to colonize plant tissues where oxygen is a limiting factor.
Lira, Nayara Patricia Vieira De; Pauletti, Bianca Alves; Marques, Ana Carolina; Perez, Carlos Alberto; Caserta, Raquel; Souza, Alessandra Alves De; Vercesi, Aníbal Eugênio; Leme, Adriana Franco Paes; Benedetti, Celso Eduardo
BigR is a sulfide sensor that regulates a sulfur transferase/dioxygenase required for aerobic respiration of plant bacteria under sulfide stress Journal Article
In: Scientific Reports 2018 8:1, vol. 8, iss. 1, pp. 1-13, 2018, ISSN: 2045-2322.
Abstract | Links | BibTeX | Tags: Biotic, Pathogens
@article{nokey,
title = {BigR is a sulfide sensor that regulates a sulfur transferase/dioxygenase required for aerobic respiration of plant bacteria under sulfide stress},
author = {Nayara Patricia Vieira De Lira and Bianca Alves Pauletti and Ana Carolina Marques and Carlos Alberto Perez and Raquel Caserta and Alessandra Alves De Souza and Aníbal Eugênio Vercesi and Adriana Franco Paes Leme and Celso Eduardo Benedetti},
url = {https://www.nature.com/articles/s41598-018-21974-x},
doi = {10.1038/s41598-018-21974-x},
issn = {2045-2322},
year = {2018},
date = {2018-01-01},
journal = {Scientific Reports 2018 8:1},
volume = {8},
issue = {1},
pages = {1-13},
publisher = {Nature Publishing Group},
abstract = {To cope with toxic levels of H2S, the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens employ the bigR operon to oxidize H2S into sulfite. The bigR operon is regulated by the transcriptional repressor BigR and it encodes a bifunctional sulfur transferase (ST) and sulfur dioxygenase (SDO) enzyme, Blh, required for H2S oxidation and bacterial growth under hypoxia. However, how Blh operates to enhance bacterial survival under hypoxia and how BigR is deactivated to derepress operon transcription is unknown. Here, we show that the ST and SDO activities of Blh are in vitro coupled and necessary to oxidize sulfide into sulfite, and that Blh is critical to maintain the oxygen flux during A. tumefaciens respiration when oxygen becomes limited to cells. We also show that H2S and polysulfides inactivate BigR leading to operon transcription. Moreover, we show that sulfite, which is produced by Blh in the ST and SDO reactions, is toxic to Citrus sinensis and that X. fastidiosa-infected plants accumulate sulfite and higher transcript levels of sulfite detoxification enzymes, suggesting that they are under sulfite stress. These results indicate that BigR acts as a sulfide sensor in the H2S oxidation mechanism that allows pathogens to colonize plant tissues where oxygen is a limiting factor.},
keywords = {Biotic, Pathogens},
pubstate = {published},
tppubtype = {article}
}
To cope with toxic levels of H2S, the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens employ the bigR operon to oxidize H2S into sulfite. The bigR operon is regulated by the transcriptional repressor BigR and it encodes a bifunctional sulfur transferase (ST) and sulfur dioxygenase (SDO) enzyme, Blh, required for H2S oxidation and bacterial growth under hypoxia. However, how Blh operates to enhance bacterial survival under hypoxia and how BigR is deactivated to derepress operon transcription is unknown. Here, we show that the ST and SDO activities of Blh are in vitro coupled and necessary to oxidize sulfide into sulfite, and that Blh is critical to maintain the oxygen flux during A. tumefaciens respiration when oxygen becomes limited to cells. We also show that H2S and polysulfides inactivate BigR leading to operon transcription. Moreover, we show that sulfite, which is produced by Blh in the ST and SDO reactions, is toxic to Citrus sinensis and that X. fastidiosa-infected plants accumulate sulfite and higher transcript levels of sulfite detoxification enzymes, suggesting that they are under sulfite stress. These results indicate that BigR acts as a sulfide sensor in the H2S oxidation mechanism that allows pathogens to colonize plant tissues where oxygen is a limiting factor.