CaMPK9 increases the stability of CaWRKY40 transcription factor which triggers defense response in chickpea upon Fusarium oxysporum f. sp. ciceri Race1 infection

2019 ◽  
Vol 100 (4-5) ◽  
pp. 411-431 ◽  
Author(s):  
Joydeep Chakraborty ◽  
Prithwi Ghosh ◽  
Senjuti Sen ◽  
Ashis Kumar Nandi ◽  
Sampa Das
Keyword(s):  
Transcription Factor ◽  
Fusarium Oxysporum ◽  
Defense Response ◽  
The Stability

scholarly journals Unraveling the Metabolite Signature of Endophytic Bacillus velezensis Strain Showing Defense Response Towards Fusarium oxysporum

Agronomy ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 683
Author(s):  
Yang Cao ◽  
Wei Ding ◽  
Chang Liu
Keyword(s):  
Fusarium Oxysporum ◽  
Inhibitory Activity ◽  
Defense Response ◽  
Endophytic Bacteria ◽  
Rice Seedling ◽  
Seedling Blight ◽  
Bacillus Velezensis ◽  
Secondary Bile Acid ◽  
Pathogen Inhibition

Seedling blight, caused by the fungus Fusarium oxysporum, significantly lowers rice production globally. Earlier reports have opined that endophytic bacteria strains could be possible biocontrol agents, but the mechanistic actions involved are still unclear. Therefore, this study aimed to isolate the endophytic bacteria with high inhibitory activity and elucidate its possible mechanisms for inducing resistance by metabolomics. The results showed that mdj-36 had the strongest in vitro pathogen inhibition of F. oxysporum, while mdj-34 displayed the lowest inhibitory activity identified as Bacillus velezensis strains. Metabolomic analyses demonstrated that B. velezensis mdj-36 growth medium could produce higher organic acids, terpenes, and diterpene than B. velezensis mdj-34. Further investigation revealed that ‘secondary bile acid biosynthesis’ and ‘glycerophospholipid metabolism’ pathways played essential roles in defense response towards F. oxysporum. This study’s findings provide a credible theoretical basis for the possible use of the B. velezensis strain against rice seedling blight.

scholarly journals UBC9 Regulates the Stability of XBP1, a Key Transcription Factor Controlling the ER Stress Response

2013 ◽  
pp. 67-79 ◽  
Author(s):  
Aya Uemura ◽  
Mai Taniguchi ◽  
Yusaku Matsuo ◽  
Masaya Oku ◽  
Sadao Wakabayashi ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Stress Response ◽  
Er Stress ◽  
Er Stress Response ◽  
The Stability

scholarly journals Induction of Defense-Related Enzymes in Banana Plants: Effect of Live and Dead Pathogenic Strain of Fusarium oxysporum f. sp. cubense

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Janki N. Thakker ◽  
Samiksha Patel ◽  
Pinakin C. Dhandhukia
Keyword(s):  
Enzyme Activity ◽  
Fusarium Oxysporum ◽  
Defense Response ◽  
Biocontrol Agent ◽  
Potential Candidate ◽  
Marker Enzyme ◽  
Panama Disease ◽  
Disease Response ◽  
Subsequent Exposure ◽  
Plant Vaccine

The aim of the present study was to scrutinize the response of banana (Grand Naine variety) plants when interacting with dead or live pathogen, Fusarium oxysporum f.sp. cubense, a causative agent of Panama disease. Response of plants was evaluated in terms of induction of defense-related marker enzyme activity, namely, peroxidase (POX), polyphenol oxidase (PPO), -1,3 glucanase, chitinase, and phenolics. Plant's interaction with live pathogen resulted in early induction of defense to restrain penetration as well as antimicrobial productions. However, pathogen overcame the defense of plant and caused disease. Interaction with dead pathogen resulted in escalating defense response in plants. Later on plants inoculated with dead pathogen showed resistance to even forced inoculation of live pathogen. Results obtained in the present study suggest that dead pathogen was able to mount defense response in plants and provide resistance to Panama disease upon subsequent exposure. Therefore, preparation from dead pathogen could be a potential candidate as a biocontrol agent or plant vaccine to combat Panama disease.

Dual regulation of transcription factor Nrf2 by Keap1 and by the combined actions of β-TrCP and GSK-3

2015 ◽  
Vol 43 (4) ◽  
pp. 611-620 ◽  
Author(s):  
John D. Hayes ◽  
Sudhir Chowdhry ◽  
Albena T. Dinkova-Kostova ◽  
Calum Sutherland
Keyword(s):  
Transcription Factor ◽  
Growth Factors ◽  
Ubiquitin Ligase ◽  
Molecular Mechanisms ◽  
Glycogen Synthase ◽  
Proteasomal Degradation ◽  
Regulation Of Transcription ◽  
Related Factor ◽  
Nrf2 Target Gene ◽  
The Stability

Nuclear factor-erythroid 2 p45 (NF-E2 p45)-related factor 2 (Nrf2) is a master regulator of redox homoeostasis that allows cells to adapt to oxidative stress and also promotes cell proliferation. In this review, we describe the molecular mechanisms by which oxidants/electrophilic agents and growth factors increase Nrf2 activity. In the former case, oxidants/electrophiles increase the stability of Nrf2 by antagonizing the ability of Kelch-like ECH-associated protein 1 (Keap1) to target the transcription factor for proteasomal degradation via the cullin-3 (Cul3)–RING ubiquitin ligase CRLKeap1. In the latter case, we speculate that growth factors increase the stability of Nrf2 by stimulating phosphoinositide 3-kinase (PI3K)−protein kinase B (PKB)/Akt signalling, which in turn results in inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3) and in doing so prevents the formation of a DSGIS motif-containing phosphodegron in Nrf2 that is recognized by the β-transducin repeat-containing protein (β-TrCP) Cul1-based E3 ubiquitin ligase complex SCFβ-TrCP. We present data showing that in the absence of Keap1, the electrophile tert-butyl hydroquinone (tBHQ) can stimulate Nrf2 activity and induce the Nrf2-target gene NAD(P)H:quinone oxidoreductase-1 (NQO1), whilst simultaneously causing inhibitory phosphorylation of GSK-3β at Ser9. Together, these observations suggest that tBHQ can suppress the ability of SCFβ-TrCP to target Nrf2 for proteasomal degradation by increasing PI3K−PKB/Akt signalling. We also propose a scheme that explains how other protein kinases that inhibit GSK-3 could stimulate induction of Nrf2-target genes by preventing formation of the DSGIS motif-containing phosphodegron in Nrf2.

scholarly journals Degradation of the Transcription Factor Gcn4 Requires the Kinase Pho85 and the SCFCDC4 Ubiquitin–Ligase Complex

2000 ◽  
Vol 11 (3) ◽  
pp. 915-927 ◽  
Author(s):  
Ariella Meimoun ◽  
Tsvi Holtzman ◽  
Ziva Weissman ◽  
Helen J. McBride ◽  
David J. Stillman ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Transcription Factor ◽  
Ubiquitin Ligase ◽  
Protein A ◽  
Purine Biosynthesis ◽  
Cell Cycle Regulators ◽  
Rich Medium ◽  
Ubiquitin Ligase Complex ◽  
Ubiquitin Conjugating Enzyme ◽  
The Stability

Gcn4, a yeast transcriptional activator that promotes the expression of amino acid and purine biosynthesis genes, is rapidly degraded in rich medium. Here we report that SCFCDC4, a recently characterized protein complex that acts in conjunction with the ubiquitin-conjugating enzyme Cdc34 to degrade cell cycle regulators, is also necessary for the degradation of the transcription factor Gcn4. Degradation of Gcn4 occurs throughout the cell cycle, whereas degradation of the known cell cycle substrates of Cdc34/SCFCDC4 is cell cycle regulated. Gcn4 ubiquitination and degradation are regulated by starvation for amino acids, whereas the degradation of the cell cycle substrates of Cdc34/SCFCDC4 is unaffected by starvation. We further show that unlike the cell cycle substrates of Cdc34/SCFCDC4, which require phosphorylation by the kinase Cdc28, Gcn4 degradation requires the kinase Pho85. We identify the critical target site of Pho85 on Gcn4; a mutation of this site stabilizes the protein. A specific Pho85-Pcl complex that is able to phosphorylate Gcn4 on that site is inactive under conditions under which Gcn4 is stable. Thus, Cdc34/SCFCDC4 activity is constitutive, and regulation of the stability of its various substrates occurs at the level of their phosphorylation.

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