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Arabidopsis Protein L-Isoaspartyl Methyltransferase repairs isoaspartyl damage to antioxidant enzymes and increases heat and oxidative stress tolerance

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Title Arabidopsis Protein L-Isoaspartyl Methyltransferase repairs isoaspartyl damage to antioxidant enzymes and increases heat and oxidative stress tolerance
 
Creator Ghosh, Shraboni
Kamble, Nitin Uttam
Verma, Pooja
Salvi, Prafull
Petla, Bhanu Prakash
Roy, Shweta
Rao, Venkateswara
Hazra, Abhijit
Varshney, Vishal
Kaur, Harmeet
Majee, Manoj
 
Subject antioxidant enzyme
Arabidopsis
isoaspartyl (isoAsp)
PROTEIN L ISOASPARTYL METHYLTRANSFERASE (PIMT)
protein repair
reactive oxygen species (ROS)
stress tolerance
abiotic stress
methyl esterification
 
Description Accepted date: December 12, 2019
Stressful environments accelerate the formation of isoaspartyl (isoAsp) residues in proteins, which detrimentally affect protein structure and function. The enzyme Protein L-Isoaspartyl Methyltransferase (PIMT) repairs other proteins by reverting deleterious isoAsp residues to functional aspartyl residues. PIMT function previously has been elucidated in seeds, but its role in plant survival under stress conditions remains undefined. Herein, we used molecular, biochemical, and genetic approaches, including protein overexpression and knockdown experiments, in Arabidopsis to investigate the role of PIMTs in plant growth and survival during heat and oxidative stresses. We demonstrate that these stresses increase isoAsp accumulation in plant proteins, that PIMT activity is essential for restricting isoAsp accumulation, and that both PIMT1 and PIMT2 play an important role in this restriction and Arabidopsis growth and survival. Moreover, we show that PIMT improves stress tolerance by facilitating efficient reactive oxygen species (ROS) scavenging and thereby protecting the functionality of antioxidant enzymes from isoAsp-mediated damage during stress. Specifically, biochemical and MS/MS analyses revealed that antioxidant enzymes acquire deleterious isoAsp residues during stress, which adversely affect their catalytic activities, and that PIMT repairs the isoAsp residues and thereby restores antioxidant enzyme function. Collectively, our results suggest that the PIMT-mediated protein repair system is an integral part of the stress tolerance mechanism in plants, in which PIMTs protect antioxidant enzymes that maintain proper ROS homeostasis against isoAsp-mediated damage in stressful environments.
This work was supported by a grant from Department of Biotechnology (BT/PR8000/BRB/10/1210/2013), Government of India and core grant of National Institute of Plant Genome Research. SG, NUK, AH and VV thank University Grant Commission and Council of Scientific and Industrial Research, Government of India, for research fellowships. We thank Dr. N. C. Bisht (NIPGR) for providing modified binary vector pPZP200lox. We thank technicians of NIPGR central instrumentation facility. We thank the technician Dr. Sudeep Ghosh of NIPGR proteomic facility for assisting MS/MS analysis (No. BT/INF/22/SP28268/2018)
The authors are thankful to DBT-eLibrary Consortium (DeLCON) for providing access to e-resources.
 
Date 2019-12-17T07:33:09Z
2019-12-17T07:33:09Z
2020
 
Type Article
 
Identifier Journal of Biological Chemistry, 295(3): 783-799
1083-351X
http://223.31.159.10:8080/jspui/handle/123456789/1023
http://www.jbc.org/content/early/2019/12/12/jbc.RA119.010779.abstract
10.1074/jbc.RA119.010779
 
Language en_US
 
Format application/pdf
 
Publisher American Society for Biochemistry and Molecular Biology