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Molecular cloning and expression of subunit 12: a non‐MCP and non‐ATPase subunit of the 26 S protease
Author(s) -
Dubiel Wolfgang,
Ferrell Katherine,
Dumdey Renate,
Standera Sybille,
Prehn Siegfried,
Rechsteiner Martin
Publication year - 1995
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(95)00288-k
Subject(s) - protein subunit , cloning (programming) , protease , gamma aminobutyric acid receptor subunit alpha 1 , molecular cloning , chemistry , microbiology and biotechnology , atpase , biochemistry , biology , enzyme , gene expression , g alpha subunit , gene , computer science , programming language
A cDNA encoding subunit 12 (S12) of human erythrocyte 26 S protease has been isolated, sequenced and expressed. The cDNA contains an open reading frame that encodes a 36.6 kDA protein 96% identical to mouse Mov‐34 and 67% identical to its Drosophila melanogaster homolog. Based on the high degree of sequence identity between human S12, mouse and Drosophila Mov‐34 proteins, we conclude that the Mov‐34 gene product is a component of the 26 S protease. Antibodies produced against two S12 fragments, Met 1 ‐Tyr 95 (S12 f95 ) and Met 1 ‐Leu 205 (S12 f205 ), react with S12 transferred to nitrocellulose from SDS‐PAGE. In contrast, after transfer from native gels, the epitope(s) recognized by anti‐S12 f205 is exposed in the regulatory complex but appears to be masked when the regulatory complex associates with the multicatalytic protease.