The 20S proteasome.
In contrast to our detailed knowledge of prokaryotic proteasomes, we have only a limited understanding of the prokaryotic regulators and their functional interaction with the proteasome. Most probably, we will soon learn more about the molecular structure and the mechanism of action of the prokaryotic regulators. Nevertheless, it still remains to be unravelled which signals or/and modifications transform an endogenous prokaryotic protein into a substrate of the proteasomal degradation machinery.
Zwickl
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Department of Molecular Structural Biology, Max Planck Institute for Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany.
D000251:Adenosine Triphosphatases / Q000502:physiology; D019843:Archaeal Proteins / Q000737:chemistry / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D002384:Catalysis; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000502:physiology; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D005057:Eukaryotic Cells / Q000201:enzymology; D005796:Genes; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry / Q000502:physiology; D011387:Prokaryotic Cells / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D021122:Protein Subunits; D013329:Structure-Activity Relationship
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004792:Enzyme Precursors; D009097:Multienzyme Complexes; D021122:Protein Subunits; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases