PRE3, HIGHLY HOMOLOGOUS TO THE HUMAN MAJOR HISTOCOMPATIBILITY COMPLEX-LINKED LMP2 (RING12) GENE, CODES FOR A YEAST PROTEASOME SUBUNIT NECESSARY FOR THE PEPTIDYLGLUTAMYL-PEPTIDE HYDROLYZING ACTIVITY
C. Enenkel et al., PRE3, HIGHLY HOMOLOGOUS TO THE HUMAN MAJOR HISTOCOMPATIBILITY COMPLEX-LINKED LMP2 (RING12) GENE, CODES FOR A YEAST PROTEASOME SUBUNIT NECESSARY FOR THE PEPTIDYLGLUTAMYL-PEPTIDE HYDROLYZING ACTIVITY, FEBS letters, 341(2-3), 1994, pp. 193-196
20S proteasomes are multifunctional proteinase complexes ubiquitous in
eucaryotes. We have cloned the yeast PPE3 gene by complementation of
the pre3-2 mutation, which leads to a defect in the peptidylglutamyl-p
eptide hydrolyzing activity of the 20S proteasome. The PRE3 gene, a be
ta-type member of the proteasomal gene family, is essential for cellul
ar life and codes for a 193-amino acid proteasomal subunit with a pred
icted molecular mass of 21.2 kDa. The Pre3 protein shows striking homo
logy to the human proteasome subunits Hsdelta and Lmp2 (Ring12). Lmp2
is encoded in the major histocompatibility complex class II region imp
licating proteasomes in antigen processing.