ArticlePlant cell reports2009
A novel patatin-like protein from cotton plant, GhPat1, is co-expressed with GhLox1 during Xanthomonas campestris-mediated hypersensitive cell death.
Article in Plant cell reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Designer TALEs enable discovery of cell death-inducer genes.Plant physiology · 2024Article
- GhPLP2 Positively Regulates Cotton Resistance to Verticillium Wilt by Modulating Fatty Acid Accumulation and Jasmonic Acid Signaling Pathway.Frontiers in plant science · 2021Article
- GhERF-IIb3 regulates the accumulation of jasmonate and leads to enhanced cotton resistance to blight disease.Molecular plant pathology · 2017Article
- Diversity and variability of NOD-like receptors in fungi.Genome biology and evolution · 2014Article
- Proteomics and transcriptomics of the BABA-induced resistance response in potato using a novel functional annotation approach.BMC genomics · 2014Article
- The pepper patatin-like phospholipase CaPLP1 functions in plant cell death and defense signaling.Plant molecular biology · 2014Article
- Phospholipases in action during plant defense signaling.Plant signaling & behavior · 2011Review
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Authors and funding
8 authors at 6 institutions in 3 countries.
Funding
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Abstract
In cotton plant, Xanthomonas-induced hypersensitive response (HR) is accompanied by a lipid peroxidation process involving a 9-lipoxygenase (LOX), GhLox1. Initiation of this oxidative metabolism implies the release of the LOX substrates, or polyunsaturated fatty acids. Since patatin-like proteins (PLPs) are likely candidates for mediating the latter step, we searched for genes encoding such enzymes, identified and cloned one of them that we named GhPat1. Biochemical and molecular studies showed that GhPat1 expression was up-regulated during the incompatible interaction, prior to the onset of the corresponding galactolipase activity and cell death symptoms in tissues. Protein sequence analysis and modelling also revealed that GhPat1 catalytic amino acids and fold were conserved across plant PLPs. Based on these results and our previous work (Jalloul et al. in Plant J 32:1-12, 2002), a role for GhPat1, in synergy with GhLox1, during HR-specific lipid peroxidation is discussed.
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