The proteasome is a large multicatalytic proteinase that plays a role in th
e generation of peptides for presentation by major histocompatibility compl
ex class I molecules. The 20S proteolytic core of mammalian proteasomes is
assembled from a group of 17 protein subunits that generate a distinctive p
attern of spots upon two-dimensional gel electrophoresis. The genes for mos
t of these subunits have been cloned from humans and rats. We isolated cDNA
clones for the mouse orthologues of ten of the subunits [PSMA1 (C2), PSMA2
(C3), PSMA3 (C8), PSMA4 (C9), PSMA5 (ZETA), PSMA6 (IOTA), PSMA7 (C6-I), PS
MB2 (C7-I), PSMB3 (C10-II), and PSMB5 (X)] to complete the cloning of all o
f the mouse subunits. Using antisera raised against these subunits or their
orthologues, we verified the identity of these proteins by two-dimensional
NEPHGE-PAGE.