scholarly journals Role of phytohormones (indol acetic acid, jasmonic acid, salcylic acid, and ethylene) in nematode-plant interactions

2017 ◽  
Vol 12 (19) ◽  
pp. 1612-1617
Author(s):  
Asefa Zebire Degife
2009 ◽  
Vol 22 (7) ◽  
pp. 763-772 ◽  
Author(s):  
Caroline Gutjahr ◽  
Uta Paszkowski

Work on the interaction of aerial plant parts with pathogens has identified the signaling molecules jasmonic acid (JA) and salicylic acid (SA) as important players in induced defense of the plant against invading organisms. Much less is known about the role of JA and SA signaling in root infection. Recent progress has been made in research on plant interactions with biotrophic mutualists and parasites that exclusively associate with roots, namely arbuscular mycorrhizal and rhizobial symbioses on one hand and nematode and parasitic plant interactions on the other hand. Here, we review these recent advances relating JA and SA signaling to specific stages of root colonization and discuss how both signaling molecules contribute to a balance between compatibility and defense in mutualistic as well as parasitic biotroph-root interactions.


Nematology ◽  
2019 ◽  
Vol 21 (2) ◽  
pp. 171-180
Author(s):  
Victoria V. Seiml-Buchinger ◽  
Svetlana V. Zinovieva ◽  
Zhanna V. Udalova ◽  
Elizaveta M. Matveeva

Summary Molecular aspects of the responses of tomato (Solanum lycopersicum) plants to invasion by Meloidogyne incognita, as well as the nematode reproduction capacity, were investigated and the role of jasmonic acid (JA) in these interactions was evaluated. Real-time quantitative PCR analysis showed that resistant and susceptible plants had similar levels of Mi1.2, PR1 and PR6 gene expression in stress-free conditions. During nematode invasion resistant plants showed up-regulation of Mi1.2, PR1 and PR6 genes and no reproduction of M. incognita. By contrast, susceptible plants showed no response in gene expression and the nematode had a high level of reproduction. Treatment of tomato plants with JA modulated Mi1.2 and PR6 gene expression that was accompanied by a suppression of the M. incognita reproduction on the roots of JA-treated susceptible plants.


Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
FM de-Faria ◽  
A Luiz-Ferreira ◽  
ACA Almeida ◽  
V Barbastefano ◽  
MA Silva ◽  
...  

Author(s):  
Bernardo Augusto Farah Santos ◽  
Rhuan Costa Souza ◽  
Maria Eduarda Dias Serenario ◽  
Eugenio Pena Mendes Junior ◽  
Thiago Araujo Simões ◽  
...  

2021 ◽  
Author(s):  
Yu Wang ◽  
Geng Wang ◽  
Jie Bai ◽  
Ning Zhao ◽  
Qingbo Wang ◽  
...  

1950 ◽  
Vol 184 (2) ◽  
pp. 755-767 ◽  
Author(s):  
Norman S. Radin ◽  
D. Rittenberg ◽  
David Shemin
Keyword(s):  

2020 ◽  
Vol 34 (11) ◽  
pp. 14647-14655
Author(s):  
Yuxin Song ◽  
Boquan Chen ◽  
Xiaomin Hu ◽  
Qiao Wang ◽  
Xingyue Xie ◽  
...  

Author(s):  
Mouna Ghorbel ◽  
Faiçal Brini ◽  
Anket Sharma ◽  
Marco Landi
Keyword(s):  

2013 ◽  
Vol 454 (3) ◽  
pp. 585-595 ◽  
Author(s):  
Joana Sá-Pessoa ◽  
Sandra Paiva ◽  
David Ribas ◽  
Inês Jesus Silva ◽  
Sandra Cristina Viegas ◽  
...  

In the present paper we describe a new carboxylic acid transporter in Escherichia coli encoded by the gene yaaH. In contrast to what had been described for other YaaH family members, the E. coli transporter is highly specific for acetic acid (a monocarboxylate) and for succinic acid (a dicarboxylate), with affinity constants at pH 6.0 of 1.24±0.13 mM for acetic acid and 1.18±0.10 mM for succinic acid. In glucose-grown cells the ΔyaaH mutant is compromised for the uptake of both labelled acetic and succinic acids. YaaH, together with ActP, described previously as an acetate transporter, affect the use of acetic acid as sole carbon and energy source. Both genes have to be deleted simultaneously to abolish acetate transport. The uptake of acetate and succinate was restored when yaaH was expressed in trans in ΔyaaH ΔactP cells. We also demonstrate the critical role of YaaH amino acid residues Leu131 and Ala164 on the enhanced ability to transport lactate. Owing to its functional role in acetate and succinate uptake we propose its assignment as SatP: the Succinate–Acetate Transporter Protein.


Sign in / Sign up

Export Citation Format

Share Document