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Arabidopsis OTU 1, a linkage‐specific deubiquitinase, is required for endoplasmic reticulum ‐associated protein degradation
Author(s) -
Zang Yuepeng,
Gong Yingya,
Wang Qian,
Guo Huiping,
Xiao Wei
Publication year - 2020
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.14524
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , arabidopsis , deubiquitinating enzyme , ubiquitin , arabidopsis thaliana , biology , microbiology and biotechnology , protein degradation , mutant , biochemistry , unfolded protein response , gene
Summary Endoplasmic reticulum ( ER )‐associated degradation ( ERAD ) is part of the ER protein quality‐control system ( ERQC ), which is critical for the conformation fidelity of most secretory and membrane proteins in eukaryotic organisms. ERAD is thought to operate in plants with core machineries highly conserved to those in human and yeast; however, little is known about the plant ERAD system. Here we report the characterization of a close homolog of human OTUB 1 in Arabidopsis thaliana , designated as At OTU 1. At OTU 1 selectively hydrolyzes several types of ubiquitin chains and these activities depend on its conserved protease domain and/or the unique N‐terminus. The otu1 null mutant is sensitive to high salinity stress, and particularly agents that cause protein misfolding. It turns out that At OTU 1 is required for the processing of known plant ERAD substrates such as barley powdery mildew O ( MLO ) alleles by virtue of its association with the CDC 48 complex through its N‐terminal region. These observations collectively define At OTU 1 as an OTU domain‐containing deubiquitinase involved in Arabidopsis ERAD .