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The 26S proteasome: Ubiquitin‐mediated proteolysis in the tunnel
Author(s) -
Kierszenbaum Abraham L.
Publication year - 2000
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/1098-2795(200010)57:2<109::aid-mrd1>3.0.co;2-9
Subject(s) - proteasome , proteolysis , protease , biology , ubiquitin , microbiology and biotechnology , proteases , intracellular , cytoplasm , protein degradation , biochemistry , enzyme , gene
The 26S proteasome is a self‐compartmentalizing protease responsible for the degradation of intracellular proteins. This giant intracellular protease is formed by several subunits arranged into two 19S polar caps—where protein recognition and ATP‐dependent unfolding occur—flanking a 20S central barrel‐shaped structure with an inner proteolytic chamber. Proteins targeted to the 26S proteasome are conjugated with a polyubiquitin chain by an enzymatic cascade before delivery to the 26S proteasome for degradation into oligopeptides. As a self‐compartmentalizing protease, the 26S proteasome circumvents proteins not destined for degradation and can be deployed to the cytoplasmic and nuclear compartments. The 26S proteasome is a representative of emerging group of giant proteases, including tricorn protease, multicorn protease, and TPPII (tripeptidyl peptidase II). Mol. Reprod. Dev. 57:109–110, 2000. © 2000 Wiley‐Liss, Inc.