Wheat Stripe Rust Resistance Protein WKS1 Reduces the Ability of the Thylakoid-Associated Ascorbate Peroxidase to Detoxify Reactive Oxygen Species. Issue 6 (19th May 2015)
- Record Type:
- Journal Article
- Title:
- Wheat Stripe Rust Resistance Protein WKS1 Reduces the Ability of the Thylakoid-Associated Ascorbate Peroxidase to Detoxify Reactive Oxygen Species. Issue 6 (19th May 2015)
- Main Title:
- Wheat Stripe Rust Resistance Protein WKS1 Reduces the Ability of the Thylakoid-Associated Ascorbate Peroxidase to Detoxify Reactive Oxygen Species
- Authors:
- Gou, Jin-Ying
Li, Kun
Wu, Kati
Wang, Xiaodong
Lin, Huiqiong
Cantu, Dario
Uauy, Cristobal
Dobon-Alonso, Albor
Midorikawa, Takamufi
Inoue, Kentaro
Sánchez, Juan
Fu, Daolin
Blechl, Ann
Wallington, Emma
Fahima, Tzion
Meeta, Madhu
Epstein, Lynn
Dubcovsky, Jorge - Abstract:
- Abstract : The wheat WKS1 protein reduces the activity of a chloroplast enzyme that detoxifies reactive oxygen species and causes cell death in the infected regions, conferring partial resistance to stripe rust. Abstract: Stripe rust is a devastating fungal disease of wheat caused by Puccinia striiformis f. sp tritici ( Pst ). The WHEAT KINASE START1 ( WKS1 ) resistance gene has an unusual combination of serine/threonine kinase and START lipid binding domains and confers partial resistance to Pst . Here, we show that wheat ( Triticum aestivum ) plants transformed with the complete WKS1 (variant WKS1.1 ) are resistant to Pst, whereas those transformed with an alternative splice variant with a truncated START domain ( WKS1.2 ) are susceptible. WKS1.1 and WKS1.2 preferentially bind to the same lipids (phosphatidic acid and phosphatidylinositol phosphates) but differ in their protein-protein interactions. WKS1.1 is targeted to the chloroplast where it phosphorylates the thylakoid-associated ascorbate peroxidase (tAPX) and reduces its ability to detoxify peroxides. Increased expression of WKS1.1 in transgenic wheat accelerates leaf senescence in the absence of Pst . Based on these results, we propose that the phosphorylation of tAPX by WKS1.1 reduces the ability of the cells to detoxify reactive oxygen species and contributes to cell death. This response takes several days longer than typical hypersensitive cell death responses, thus allowing the limited pathogen growth andAbstract : The wheat WKS1 protein reduces the activity of a chloroplast enzyme that detoxifies reactive oxygen species and causes cell death in the infected regions, conferring partial resistance to stripe rust. Abstract: Stripe rust is a devastating fungal disease of wheat caused by Puccinia striiformis f. sp tritici ( Pst ). The WHEAT KINASE START1 ( WKS1 ) resistance gene has an unusual combination of serine/threonine kinase and START lipid binding domains and confers partial resistance to Pst . Here, we show that wheat ( Triticum aestivum ) plants transformed with the complete WKS1 (variant WKS1.1 ) are resistant to Pst, whereas those transformed with an alternative splice variant with a truncated START domain ( WKS1.2 ) are susceptible. WKS1.1 and WKS1.2 preferentially bind to the same lipids (phosphatidic acid and phosphatidylinositol phosphates) but differ in their protein-protein interactions. WKS1.1 is targeted to the chloroplast where it phosphorylates the thylakoid-associated ascorbate peroxidase (tAPX) and reduces its ability to detoxify peroxides. Increased expression of WKS1.1 in transgenic wheat accelerates leaf senescence in the absence of Pst . Based on these results, we propose that the phosphorylation of tAPX by WKS1.1 reduces the ability of the cells to detoxify reactive oxygen species and contributes to cell death. This response takes several days longer than typical hypersensitive cell death responses, thus allowing the limited pathogen growth and restricted sporulation that is characteristic of the WKS1 partial resistance response to Pst. … (more)
- Is Part Of:
- The Plant Cell. Volume 27:Issue 6(2015)
- Journal:
- The Plant Cell
- Issue:
- Volume 27:Issue 6(2015)
- Issue Display:
- Volume 27, Issue 6 (2015)
- Year:
- 2015
- Volume:
- 27
- Issue:
- 6
- Issue Sort Value:
- 2015-0027-0006-0000
- Page Start:
- 1755
- Page End:
- 1770
- Publication Date:
- 2015-05-19
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.134296 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16317.xml