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 |
|---|---|
| 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