Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


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



ID: 318575.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Proteasomes and other self-compartmentalizing proteases in prokaryotes
Authors:De Mot, R.; Nagy, I.; Walz, J.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1999
Title of Journal:Trends in Microbiology.
Volume:7
Issue / Number:2
Start Page:88
End Page:92
Audience:Not Specified
Abstract / Description:The proteasome represents the major non-lysosomal proteolytic system in eukaryotes. It confines proteolytic activity to an inner compartment that is accessible to unfolded proteins only. The strategy of controlling intracellular breakdown of proteins by self-compartmentalization is also used by different types of prokaryotic energy-dependent proteases. Genomic sequencing data reveal that various combinations of these energy-dependent proteases occur in prokaryotic cells from different lineages. [References: 33]
Free Keywords:Adenosinetriphosphatase/ge [Genetics]; Adenosinetriphosphatase/me [Metabolism]; *Archaea/en [Enzymology]; Archaea/ge [Genetics]; Archaea/ul [Ultrastructure]; *Bacteria/en [Enzymology]; Bacteria/ge [Genetics]; Bacteria/ul [Ultrastructure]; *Cysteine Endopeptidases/ge [Genetics]; *Cysteine Endopeptidases/me [Metabolism]; Endopeptidases/ge [Genetics]; *Endopeptidases/me [Metabolism]; *Multienzyme Complexes/ge [Genetics]; *Multienzyme Complexes/me [Metabolism]; Support, Non-U.S. Gov't
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.