A giant protease with potential to substitute for some functions of the proteasome

被引：304

作者：

Geier, E

Pfeifer, G

Wilm, M

Lucchiari-Hartz, M

Baumeister, W

Eichmann, K

Niedermann, G

机构：

[1] Max Planck Inst Immunobiol, D-79108 Freiburg, Germany

[2] Max Planck Inst Biochem, D-82152 Martinsried, Germany

[3] European Mol Biol Lab, D-69117 Heidelberg, Germany

来源：

SCIENCE | 1999年 / 283卷 / 5404期

关键词：

D O I：

10.1126/science.283.5404.978

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An alanyl-alanyl-phenylalanyl-7-amino-4-methylcoumarin-hydrolyzing protease particle copurifying with 265 proteasomes was isolated and identified as tripeptidyl peptidase II(TPPII), a cytosolic subtilisin-like peptidase of unknown function. The particle is larger than the 265 proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like endoproteolytic cleavage. TPPII may thus participate in extralysosomal polypeptide degradation and may in part account for nonproteasomal epitope generation as postulated for certain major histocompatibility complex class I alleles, In addition, TPPII may be able to substitute for some metabolic functions of the proteasome.

引用

页码：978 / 981

页数：4

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