Ubiquitin-specific protease16 interacts with a heavy metal associated isoprenylated plant protein27 and modulates cadmium tolerance

Abstract

Protein ubiquitination and deubiquitination are two reversible processes catalyzed by ubiquitin ligases and deubiq-uitinating enzymes, respectively. in Arabidopsis, lots of substrates of ubiquitin ligases were found, whereas only a few targets of deubiquitinating enzymes were identifed. recently, we reported that a functional uBiQuitin-SPECiFiC Pro-tEaSE16 (uBP16) was involved in salt tolerance through positively regulating plasma membrane na+/h+ antiport activity and at least partially modulating SErinE hYDroXYmEthYLtranSFEraSE1 (Shm1) stability and activity. here, we report that uBP16 interacts with hEaVY mEtaL aSSoCiatED iSoPrEnYLatED PLant ProtEin27 (hiPP27), a metallochaperone containing a predicted heavy-metal-associated domain, which has been reported to play an important role in cadmium detoxifcation. meanwhile, the ubp16 mutant showed more sensitive to cadmium than wild-type. taken together, hiPP27 may be another target of uBP16 in cadmium response. © 2013 Landes Bioscience.