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Li, Jing,Liu, Juntao,Wang, Guoqiang,Cha, Joon-Yung,Li, Guannan,Chen, She,Li, Zhen,Guo, Jinghua,Zhang, Caiguo,Yang, Yongqing,Kim, Woe-Yeon,Yun, Dae-Jin,Schumaker, Karen S.,Chen, Zhongzhou,Guo, Yan American Society of Plant Biologists 2015 The Plant cell Vol.27 No.3
<P>Arabidopsis protein NCA1 interacts with catalases in the cytosol and increases catalase activity through maintaining catalase folding state, which is required for stress responses.</P><P>Catalases are key regulators of reactive oxygen species homeostasis in plant cells. However, the regulation of catalase activity is not well understood. In this study, we isolated an <I>Arabidopsis thaliana</I> mutant, <I>no catalase activity1-3</I> (<I>nca1-3</I>) that is hypersensitive to many abiotic stress treatments. The mutated gene was identified by map-based cloning as NCA1, which encodes a protein containing an N-terminal RING-finger domain and a C-terminal tetratricopeptide repeat-like helical domain. NCA1 interacts with and increases catalase activity maximally in a 240-kD complex in planta. In vitro, NCA1 interacts with CATALASE2 (CAT2) in a 1:1 molar ratio, and the NCA1 C terminus is essential for this interaction. CAT2 activity increased 10-fold in the presence of NCA1, and zinc ion binding of the NCA1 N terminus is required for this increase. NCA1 has chaperone protein activity that may maintain the folding of catalase in a functional state. NCA1 is a cytosol-located protein. Expression of <I>NCA1</I> in the mitochondrion of the <I>nca1-3</I> mutant does not rescue the abiotic stress phenotypes of the mutant, while expression in the cytosol or peroxisome does. Our results suggest that NCA1 is essential for catalase activity.</P>