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Trp Oxidation Singlet Oxygen

Carbonylation in Arabidopsis thaliana

9 modifications in 9 peptides, found in 7 proteins

Experiment Details

Exp 122


Experimental Setup
Tissue3-week old plants, EX1-GFP ex1 flu
ConditionDark or continuous light-grown seedlings
MS InstrumentQ Exactive
MS/MS Search Parameters
Protein DatabaseTAIR10
Decoy StrategyReverse database
FDR Threshold0.01
Search Algorithm(s)MaxQuant
Precursor Mass Tolerance7 ppm
PTM Site AllocationPTM Score
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsOxidation (MFYH)
Phosphorylation (STY)
Other Information
CommentsTable 1. Intermediate Trp oxidation products also observed: keto-amino-hydroxy derivative oxindolylalanine (+16), a dihydro-hydroxy derivative N-formylkynurenine (+32), and kynurenine (+ 4 Da).


Publication Information

Dogra et al. 2019

PubMed ID: 31249292

No external accession available

Abstract

Nat Commun. 2019 Jun 27;10(1):2834. doi: 10.1038/s41467-019-10760-6.

Oxidative post-translational modification of EXECUTER1 is required for singlet 
oxygen sensing in plastids.

Dogra V(1), Li M(1)(2), Singh S(1), Li M(1)(2), Kim C(3)(4).

Author information:
(1)Shanghai Center for Plant Stress Biology and Center of Excellence in 
Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.
(2)University of the Chinese Academy of Sciences, 100049, Beijing, China.
(3)Shanghai Center for Plant Stress Biology and Center of Excellence in 
Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China. 
chanhongkim@sibs.ac.cn.
(4)University of the Chinese Academy of Sciences, 100049, Beijing, China. 
chanhongkim@sibs.ac.cn.

Environmental information perceived by chloroplasts can be translated into 
retrograde signals that alter the expression of nuclear genes. Singlet oxygen 
(1O2) generated by photosystem II (PSII) can cause photo-oxidative damage of 
PSII but has also been implicated in retrograde signaling. We previously 
reported that a nuclear-encoded chloroplast FtsH2 metalloprotease coordinates 
1O2-triggered retrograde signaling by promoting the degradation of the EXECUTER1 
(EX1) protein, a putative 1O2 sensor. Here, we show that a 1O2-mediated 
oxidative post-translational modification of EX1 is essential for initiating 
1O2-derived signaling. Specifically, the Trp643 residue in DUF3506 domain of EX1 
is prone to oxidation by 1O2. Both the substitution of Trp643 with 
1O2-insensitive amino acids and the deletion of the DUF3506 domain abolish the 
EX1-mediated 1O2 signaling. We thus provide mechanistic insight into how EX1 
senses 1O2 via Trp643 located in the DUF3506 domain.

DOI: 10.1038/s41467-019-10760-6
PMCID: PMC6597547
PMID: 31249292 [Indexed for MEDLINE]

Conflict of interest statement: The authors declare no competing interests.