作者: M Rechsteiner , C Realini , W Dubiel , K Ferrell , G Pratt
DOI: 10.1016/S0021-9258(17)32052-5
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摘要: The multicatalytic protease (MCP) can be activated by two distinct multisubunit complexes. One is the regulatory component of 26 S protease, which contains at least 15 subunits. other a hexameric activator composed 31- and 29-kDa A cDNA for smaller subunit has been cloned sequenced. encodes protein 249 amino acids. Embedded between sequences typical globular domains stretch 28 "alternating" lysine glutamic acid residues. Similar regions, we call KEKE motifs, are also found in MCP subunits, 12 variety chaperonins including hsp90, hsp70, calnexin. Expression Escherichia coli produced functional virtually indistinguishable from purified directly red blood cells. recombinant formed three isoelectric species on two-dimensional polyacrylamide gel electrophoresis, it reacted with antibodies to cell activator. Recombinant bound stimulated cleavage carboxyl terminus hydrophobic or charged Synthesis was induced gamma interferon treatment HeLa These last findings have implications antigen presentation class I major histocompatibility receptors.