The Rice TAL Effector–Dependent Resistance Protein XA10 Triggers Cell Death and Calcium Depletion in the Endoplasmic Reticulum. Issue 1 (31st January 2014)

• Record Type: Journal Article
• Authors: Tian, Dongsheng; Wang, Junxia; Zeng, Xuan; Gu, Keyu; Qiu, Chengxiang; Yang, Xiaobei; Zhou, Zhiyun; Goh, Meiling; Luo, Yanchang; Murata-Hori, Maki; White, Frank F.; Yin, Zhongchao
• Is Part Of: The Plant Cell. Volume 26:Issue 1(2014)
• Page Start: 497
• Page End: 515
• Publication Date: 2014-01-31
• DOI: 10.1105/tpc.113.119255
• Languages: English
• ISSNs: 1040-4651

Abstract

Abstract : This work identifies and characterizes a rice disease resistance gene, XA10, which encodes an inducible, intrinsic terminator protein that triggers programmed cell death in plant and animal cells. This cell death involves disruption of the endoplasmic reticulum and cellular Ca 2+ homeostasis. Abstract: The recognition between disease resistance ( R ) genes in plants and their cognate avirulence ( Avr ) genes in pathogens can produce a hypersensitive response of localized programmed cell death. However, our knowledge of the early signaling events of the R gene–mediated hypersensitive response in plants remains limited. Here, we report the cloning and characterization of Xa10, a transcription activator–like (TAL ) effector-dependent R gene for resistance to bacterial blight in rice ( Oryza sativa ). Xa10 contains a binding element for the TAL effector AvrXa10 ( EBE AvrXa10 ) in its promoter, and AvrXa10 specifically induces Xa10 expression. Expression of Xa10 induces programmed cell death in rice, Nicotiana benthamiana, and mammalian HeLa cells. The Xa10 gene product XA10 localizes as hexamers in the endoplasmic reticulum (ER) and is associated with ER Ca 2+ depletion in plant and HeLa cells. XA10 variants that abolish programmed cell death and ER Ca 2+ depletion in N. benthamiana and HeLa cells also abolish disease resistance in rice. We propose that XA10 is an inducible, intrinsic terminator protein that triggers programmed cell death by a conserved mechanism involving disruption of the ER and cellular Ca 2+ homeostasis.