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Environmental information perceived by chloroplasts can be translated into retrograde signals that alter the expression of nuclear genes. Singlet oxygen ( 1 O 2 ) 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  1 O 2 -triggered retrograde signaling by promoting the degradation of the EXECUTER1 (EX1) protein, a putative  1 O 2  sensor. Here, we show that a  1 O 2 -mediated oxidative post-translational modification of EX1 is essential for initiating  1 O 2 -derived signaling. Specifically, the Trp643 residue in DUF3506 domain of EX1 is prone to oxidation by  1 O 2 . Both the substitution of Trp643 with  1 O 2 -insensitive amino acids and the deletion of the DUF3506 domain abolish the EX1-mediated  1 O 2  signaling. We thus provide mechanistic insight into how EX1 senses  1 O 2  via Trp643 located in the DUF3506 domain.

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