Genetically Modified Heat Shock Protein90s and Polyamine Oxidases in Reveal Their Interaction under Heat Stress Affecting Polyamine Acetylation, Oxidation and Homeostasis of Reactive Oxygen Species.

The chaperones, heat shock proteins (HSPs), stabilize proteins to minimize proteotoxic stress, especially during heat stress (HS) and polyamine (PA) oxidases (PAOs) participate in the modulation of the cellular homeostasis of PAs and reactive oxygen species (ROS). An interesting interaction of HSP90s and PAOs was revealed in by using the line against the four genes encoding cytosolic proteins, the T-DNA and insertional mutants, the mutant and pharmacological inhibitors of HSP90s and PAOs. Silencing of all cytosolic genes resulted in several-fold higher levels of soluble spermidine (S-Spd), acetylated Spd (N-acetyl-Spd) and acetylated spermine (N-acetyl-Spm) in the transgenic leaves.