A novel patatin-like protein from cotton plant, GhPat1, is co-expressed with GhLox1 during Xanthomonas campestris-mediated hypersensitive cell death

被引:19
作者
Cacas, Jean-Luc [1 ]
Marmey, Philippe [1 ]
Montillet, Jean-Luc [2 ]
Sayegh-Alhamdia, Majd [1 ]
Jalloul, Aida [3 ]
Rojas-Mendoza, Ana [4 ]
Clerivet, Alain [5 ]
Nicole, Michel [1 ]
机构
[1] IRD, UMR RPB, F-34394 Montpellier 5, France
[2] CEA, Lab Echanges Membranaires & Signalisat, DSV DEVM, F-13108 St Paul Les Durance, France
[3] Univ Damascus, Fac Agron, Dept Plant Protect, Damascus, Syria
[4] Ctr Nacl Invest Oncol, Struct Bioinformat Grp, Madrid 28029, Spain
[5] Univ Montpellier 2, UMR RBP, F-34095 Montpellier 5, France
关键词
Patatin-like protein; Galactolipase; Lipoxygenase; Lipid peroxidation; Hypersensitive response; Programmed cell death; LIPID ACYL HYDROLASE; FATTY-ACID HYDROPEROXIDES; ARABIDOPSIS-THALIANA; GENE-EXPRESSION; TOBACCO-LEAVES; LIPOXYGENASE GENE; CRYSTAL-STRUCTURE; BACTERIAL-BLIGHT; DROUGHT STRESS; OXYLIPINS;
D O I
10.1007/s00299-008-0622-x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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.
引用
收藏
页码:155 / 164
页数:10
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