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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318389.0, MPI für Biochemie / Structural Biology (W. Baumeister)
A giant protease with potential to substitute for some functions of the proteasome
Authors:Geier, E.; Pfeifer, G.; Wilm, M.; Lucchiari-Hartz, M.; Baumeister, W.; Eichmann, K.; Niedermann, G.
Date of Publication (YYYY-MM-DD):1999
Title of Journal:Science
Journal Abbrev.:Science
Volume:283
Issue / Number:5404
Start Page:978
End Page:981
Audience:Not Specified
Abstract / Description: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. [References: 28]
Free Keywords:Tripeptidyl-peptidase-ii; Rat-liver; Inhibition; Lactacystin; Proteins; Cells.; Multidisciplinary in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Multidisciplinary in Current Contents(R)/Life Sciences. Multidisciplinary in Current Contents(R)/Physical, Chemical & Earth Sciences.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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