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

Hilt, Wolfgang¹  Wolf, Dieter H.¹  Gückel, Roland¹  Kipper, Julia¹  Lehmann, Heike¹  Enenkel, Cordula¹ 

[1] Institut für Biochemie der Universität Stuttgart Pfaffenwaldring 55 D-70569 Stuttgart, Germany

关键词: Proteasome;    Proteolysis (yeast);    Antigen processing (human MHC);    Cbz;    benzyloxycarbonyl;    βNA;    β-naphthylamine;    MHC;    major histocompatibility complex;    PGPH;    peptidylglutamyl-peptide hydrolyzing;   

DOI  :  10.1016/0014-5793(94)80455-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

20S proteasomes are multifunctional proteinase complexes ubiquitous in eucaryotes. We have cloned the yeast PRE3 gene by complementation of the pre3-2 mutation, which leads to a defect in the peptidylglutamyl-peptide hydrolyzing activity of the 20S proteasome. The PRE3 gene, a β-type member of the proteasomal gene family, is essential for cellular life and codes for a 193-amino acid proteasomal subunit with a predicted molecular mass of 21.2 kDa. The Pre3 protein shows striking homology to the human proteasome subunits Hsδ and Lmp2 (Ring12). Lmp2 is encoded in the major histocompatibility complex class II region implicating proteasomes in antigen processing.

【 授权许可】

Unknown