The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis.
作者： W. Hilt , C. Enenkel , A. Gruhler , T. Singer , D.H. Wolf
DOI: 10.1016/S0021-9258(18)53719-4
关键词: Biology 、 Ubiquitin 、 Amino acid 、 Proteasome 、 Molecular biology 、 Biochemistry 、 Protein subunit 、 Peptide sequence 、 Mutant protein 、 Mutant 、 Peptide
摘要: Proteinase yscE, the yeast proteasome, is a member of nonlysosomal, high molecular mass (approximately 700 kDa) multifunctional proteinase complexes that are highly conserved from to man. We have isolated mutants defective in one three proteolytic activities enzyme complex, i.e. cleavage peptide bonds after acidic amino acids. Using these (pre4-1), we cloned PRE4 gene and uncovered an open reading frame with 266 acids coding for predicted protein 29.4 kDa. The proved be subunit yscE. Pre4 acid sequence shows strong homology beta-subunit Xenopus laevis proteasome. Chromosomal deletion lethal. pre4-1 mutant allele was sequenced. shortened by 15 at carboxyl terminus. Mutations (pre1-1, pre2-2) chymotrypsin-like activity yscE involved ubiquitin-linked stress-dependent pathways. In contrast mutants, did not exhibit any apparent phenotypes. However, pre1-1 double showed enhanced canavanine sensitivity increased accumulation ubiquitin conjugates, as compared single mutants.
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