Lysine acetylation is a dynamic post-translational modification of proteins. Extensive studies have revealed that the acetylation modulated by histone acetyltransferases and histone deacetylases (HDACs) plays a crucial role in regulating protein function. However, there has been limited focus on how HDACs regulate jasmonic acid (JA) biosynthesis in plants. Here, we uncover that the protein stability of OsLOX14, a critical enzyme involved in JA biosynthesis, is regulated by a histone deacetylase, OsHDA706, and is hindered by a viral protein. Our results show that OsHDA706 deacetylates OsLOX14 and enhances the stability of OsLOX14, leading to JA accumulation and an improved broad-spectrum rice antiviral defense. Furthermore, we found that the viral protein P2, encoded by the destructive rice stripe virus, disrupts the association of OsHDA706-OsLOX14, promoting viral infection. Overall, our findings reveal how HDAC manipulates the interplay of deacetylation and protein stability of a JA biosynthetic enzyme to enhance plant antiviral responses.

The fluorescence quenching technique was applied to study the interactions between lysozyme and Gold nanoparticles (GNPs). GNPs were synthesized by microwave assisted heating under reflux, using trisodium citrate as the reducing agent. The UV-visible spectra and TEM image were used to characterize the GNPs. The GNPs had a maximum absorption peak at 520 nm, with an average diameter of 13.3 nm. The fluorescence quenching mechanism was studied by Stern-Volmer equation. It was proved that the fluorescence quenching of lysozyme by GNPs was mainly a result of the formation of a lysozyme-GNP complex. Experimental results indicated that the combination reactions of GNPs and lysozyme were static quenching processes. It can be expected that the fluorescence quenching technique could provide a promising tool to study the interactions of GNPs and proteins. The binding constants, the number of binding sites at different temperatures and corresponding thermodynamic parameters ΔG, ΔH, and ΔS were also calculated.