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Electron microscopy of 26 S complex containing 20 S proteasome
Author(s) -
Atsushi Ikai,
Masaaki Nishigai,
Keiji Tanaka,
Akira Ichihara
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80824-m
Subject(s) - proteasome , electron microscope , intracellular , ubiquitin , chemistry , morphology (biology) , biophysics , protease , microbiology and biotechnology , biochemistry , crystallography , biology , enzyme , physics , genetics , optics , gene
A high molecular weight protease complex (26 S complex) involved in the intracellular protein degradation of ubiquitinated proteins was purified from rat liver and studied by electron microscopy. The most prevalent molecular species with best preserved symmetrical morphology had two large rectangular terminal structures attached to a thinner central one having four protein layers. We concluded that they were the closest representation of the 26 S complex so far reported. The central structure was identified as 20 S proteasome and the terminal one as recognition units for ubiquitinated proteins.