A chaperone function of NO CATALASE ACTIVITY1 Is required to maintain catalase activity and for multiple stress responses in arabidopsis

Jing Li, Juntao Liu, Guoqiang Wang, Joon Yung Cha, Guannan Li, She Chen, Zhen Li, Jinghua Guo, Caiguo Zhang, Yongqing Yang, Woe Yeon Kim, Dae Jin Yun, Karen S Schumaker, Zhongzhou Chen, Yan Guo

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

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 Arabidopsis thaliana mutant, no catalase activity1-3 (nca1-3) 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 NCA1 in the mitochondrion of the nca1-3 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.

Original languageEnglish (US)
Pages (from-to)908-925
Number of pages18
JournalPlant Cell
Volume27
Issue number3
DOIs
StatePublished - 2015

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Arabidopsis
Catalase
stress response
catalase
cytosol
Cytosol
mutants
abiotic stress
RING Finger Domains
Proteins
Peroxisomes
terminal repeat sequences
proteins
Terminal Repeat Sequences
Plant Cells
peroxisomes
Plantae
Zinc
Organism Cloning
molecular cloning

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

Cite this

A chaperone function of NO CATALASE ACTIVITY1 Is required to maintain catalase activity and for multiple stress responses in arabidopsis. / 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.

In: Plant Cell, Vol. 27, No. 3, 2015, p. 908-925.

Research output: Contribution to journalArticle

Li, J, Liu, J, Wang, G, Cha, JY, Li, G, Chen, S, Li, Z, Guo, J, Zhang, C, Yang, Y, Kim, WY, Yun, DJ, Schumaker, KS, Chen, Z & Guo, Y 2015, 'A chaperone function of NO CATALASE ACTIVITY1 Is required to maintain catalase activity and for multiple stress responses in arabidopsis', Plant Cell, vol. 27, no. 3, pp. 908-925. https://doi.org/10.1105/tpc.114.135095
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. / A chaperone function of NO CATALASE ACTIVITY1 Is required to maintain catalase activity and for multiple stress responses in arabidopsis. In: Plant Cell. 2015 ; Vol. 27, No. 3. pp. 908-925.
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