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

被引：73

作者：

ENENKEL, C ^{[1
]}

LEHMANN, H ^{[1
]}

KIPPER, J ^{[1
]}

GUCKEL, R ^{[1
]}

HILT, W ^{[1
]}

WOLF, DH ^{[1
]}

机构：

[1] UNIV STUTTGART,INST BIOCHEM,PFAFFENWALDRING 55,D-70569 STUTTGART,GERMANY

来源：

FEBS LETTERS | 1994年 / 341卷 / 2-3期

关键词：

PROTEASOME; PROTEOLYSIS (YEAST); ANTIGEN PROCESSING (HUMAN MHC);

D O I：

10.1016/0014-5793(94)80455-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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-peptide hydrolyzing activity of the 20S proteasome. The PRE3 gene, a beta-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 Hsdelta and Lmp2 (Ring12). Lmp2 is encoded in the major histocompatibility complex class II region implicating proteasomes in antigen processing.

引用

页码：193 / 196

页数：4

共 39 条

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