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Regulating the regulator: nitric oxide control of post‐translational modifications
Author(s) -
Gupta Kapuganti Jagadis,
Kolbert Zsuzsanna,
Durner Jorg,
Lindermayr Christian,
Corpas Francisco J.,
Brouquisse Renaud,
Barroso Juan B.,
Umbreen Saima,
Palma José M.,
Hancock John T.,
Petrivalsky Marek,
Wendehenne David,
Loake Gary J.
Publication year - 2020
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.16622
Subject(s) - nitric oxide , acetylation , regulator , sumo protein , microbiology and biotechnology , phosphorylation , cysteine , chemistry , function (biology) , biochemistry , biology , ubiquitin , organic chemistry , gene , enzyme
Summary Nitric oxide (NO) is perfectly suited for the role of a redox signalling molecule. A key route for NO bioactivity occurs via protein S ‐nitrosation, and involves the addition of a NO moiety to a protein cysteine (Cys) thiol (–SH) to form an S ‐nitrosothiol (SNO). This process is thought to underpin a myriad of cellular processes in plants that are linked to development, environmental responses and immune function. Here we collate emerging evidence showing that NO bioactivity regulates a growing number of diverse post‐translational modifications including SUMOylation, phosphorylation, persulfidation and acetylation. We provide examples of how NO orchestrates these processes to mediate plant adaptation to a variety of cellular cues.