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The ubiquitin-proteasome system is fundamentally involved in myriad biological phenomena of eukaryotes. In plants, this regulated protein degradation system has a pivotal role in the cellular response mechanisms for both internal and external stimuli, such as plant hormones and environmental stresses. Information about substrate selection by the ubiquitination machinery has accumulated, but there is very little information about selectivity for substrates at the proteasome. Here, we report characterization of a novel abscisic acid (ABA)-hypersensitive mutant named  ABA hypersensitive germination12  ( ahg12 ) in Arabidopsis. The  ahg12  mutant showed a unique pleiotropic phenotype, including hypersensitivity to ABA and ethylene, and hyposensitivity to light. Map-based cloning identified the  ahg12  mutation to cause an amino acid conversion in the L23 loop of RPT5a, which is predicted to form the pore structure of the 19S RP complex of the proteasome. Transient expression assays demonstrated that some plant-specific signaling components accumulated at higher levels in the  ahg12  mutant. These results suggest that the  ahg12  mutation led to changes in the substrate preference of the 26S proteasome. The discovery of the  ahg12  mutation thus will contribute to elucidate the characteristics of the regulated protein degradation system.

ahg12 is a dominant proteasome mutant that affects multiple regulatory systems for germination of Arabidopsis