Abstract
A key feature of the plant defence response is the transient engagement of a nitrosative burst, resulting in the synthesis of reactive nitrogen intermediates (RNIs). Specific, highly reactive cysteine (Cys) residues of low pK a are a major site of action for these intermediates. The addition of an NO moiety to a Cys thiol to form an S-nitrosothiol (SNO), is termed S-nitrosylation. This redox-based post-translational modification is emerging as a key regulator of protein function in plant immunity. Here we highlight recent advances in our understanding of de-nitrosylation, the mechanism that depletes protein SNOs, with a focus on S-nitrosoglutathione reductase (GSNOR). This enzyme controls total cellular S-nitrosylation indirectly during the defence response by turning over S-nitrosoglutathione (GSNO), a major cache of NO bioactivity.
Original language | English |
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Pages (from-to) | 540-544 |
Number of pages | 5 |
Journal | Plant Science |
Volume | 181 |
Issue number | 5 |
DOIs | |
State | Published - Nov 2011 |
Keywords
- De-nitrosylation
- Disease resistance
- GSNOR
- Plant defence response
- S-nitrosylation