Dis-assembly lines: the proteasome and related ATPase-assisted proteases.
Self-compartmentalizing proteases, such as the proteasome and several prokaryotic energy-dependent proteases, are designed to act in the crowded environment of the cell. Proteins destined for degradation are recognized and unfolded by regulatory subcomplexes that invariably contain ATPase modules, before being translocated into another subcomplex, the proteolytic core, for degradation. The sequential actions effected on substrates are reflected in the linear arrangement of these subcomplexes; thus, the holocomplexes are organized as molecular disassembly and degradation lines.
Zwickl
P
P
Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Martinsried, 82152, Germany.
Baumeister
W
W
Steven
A
A
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000502:physiology; D049071:Endopeptidase Clp; D010450:Endopeptidases / Q000737:chemistry* / Q000502:physiology; D005656:Fungal Proteins / Q000737:chemistry; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000502:physiology; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D001426:Bacterial Proteins; D005656:Fungal Proteins; D046911:Macromolecular Substances; D018832:Molecular Chaperones; D009097:Multienzyme Complexes; D010450:Endopeptidases; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases