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CLC number: S432.1

On-line Access: 2019-08-05

Received: 2019-03-01

Revision Accepted: 2019-05-12

Crosschecked: 2019-07-09

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Citations:  Bibtex RefMan EndNote GB/T7714


Yan Liang


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Journal of Zhejiang University SCIENCE B 2019 Vol.20 No.9 P.713-727


Antepenultimate residue at the C-terminus of NADPH oxidase RBOHD is critical for its function in the production of reactive oxygen species in Arabidopsis

Author(s):  Qiu-Ying Li, Ping Li, Nang Myint Phyu Sin Htwe, Ke-Ke Shangguan, Yan Liang

Affiliation(s):  Ministry of Agriculture Key Lab of Molecular Biology of Crop Pathogens and Insects, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, China

Corresponding email(s):   yanliang@zju.edu.cn

Key Words:  Reactive oxygen species (ROS), NADPH oxidase (NOX), Microbe associated molecular pattern (MAMP), Lipopolysaccharides (LPS), Respiratory burst oxidase homolog D (RBOHD)

Qiu-Ying Li, Ping Li, Nang Myint Phyu Sin Htwe, Ke-Ke Shangguan, Yan Liang. Antepenultimate residue at the C-terminus of NADPH oxidase RBOHD is critical for its function in the production of reactive oxygen species in Arabidopsis[J]. Journal of Zhejiang University Science B, 2019, 20(9): 713-727.

@article{title="Antepenultimate residue at the C-terminus of NADPH oxidase RBOHD is critical for its function in the production of reactive oxygen species in Arabidopsis",
author="Qiu-Ying Li, Ping Li, Nang Myint Phyu Sin Htwe, Ke-Ke Shangguan, Yan Liang",
journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T Antepenultimate residue at the C-terminus of NADPH oxidase RBOHD is critical for its function in the production of reactive oxygen species in Arabidopsis
%A Qiu-Ying Li
%A Ping Li
%A Nang Myint Phyu Sin Htwe
%A Ke-Ke Shangguan
%A Yan Liang
%J Journal of Zhejiang University SCIENCE B
%V 20
%N 9
%P 713-727
%@ 1673-1581
%D 2019
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1900105

T1 - Antepenultimate residue at the C-terminus of NADPH oxidase RBOHD is critical for its function in the production of reactive oxygen species in Arabidopsis
A1 - Qiu-Ying Li
A1 - Ping Li
A1 - Nang Myint Phyu Sin Htwe
A1 - Ke-Ke Shangguan
A1 - Yan Liang
J0 - Journal of Zhejiang University Science B
VL - 20
IS - 9
SP - 713
EP - 727
%@ 1673-1581
Y1 - 2019
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1900105

Production of reactive oxygen species (ROS) is a conserved immune response primarily mediated by NADPH oxidases (NOXs), also known in plants as respiratory burst oxidase homologs (RBOHs). Most microbe-associated molecular patterns (MAMPs) trigger a very fast and transient ROS burst in plants. However, recently, we found that lipopolysaccharides (LPS), a typical bacterial MAMP, triggered a biphasic ROS burst. In this study, we isolated mutants defective in LPS-triggered biphasic ROS burst (delt) in Arabidopsis, and cloned the DELT1 gene that was shown to encode RBOHD. In the delt1-2 allele, the antepenultimate residue, glutamic acid (E919), at the C-terminus of RBOHD was mutated to lysine (K). E919 is a highly conserved residue in NADPH oxidases, and a mutation of the corresponding residue E568 in human NOX2 has been reported to be one of the causes of chronic granulomatous disease. Consistently, we found that residue E919 was indispensable for RBOHD function in the MAMP-induced ROS burst and stomatal closure. It has been suggested that the mutation of this residue in other NADPH oxidases impairs the protein’s stability and complex assembly. However, we found that the E919K mutation did not affect RBOHD protein abundance or the ability of protein association, suggesting that the residue E919 in RBOHD might have a regulatory mechanism different from that of other NOXs. Taken together, our results confirm that the antepenultimate residue E is critical for NADPH oxidases and provide a new insight into the regulatory mechanisms of RBOHD.




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[57]List of electronic supplementary materials

[58]Table S1 Primer sequences used in this study

[59]Fig. S1 Allelic mutants delt1-1 and delt1-2

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