Regulation by proteolysis: energy-dependent proteases and their targets.
A number of critical regulatory proteins in both prokaryotic and eukaryotic cells are subject to rapid, energy-dependent proteolysis. Rapid degradation combined with control over biosynthesis provides a mechanism by which the availability of a protein can be limited both temporally and spatially. Highly unstable regulatory proteins are involved in numerous biological functions, particularly at the commitment steps in developmental pathways and in emergency responses. The proteases involved in energy-dependent proteolysis are large proteins with the ability to use ATP to scan for appropriate targets and degrade complete proteins in a processive manner. These cytoplasmic proteases are also able to degrade many abnormal proteins in the cell.
Gottesman
S
S
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
Maurizi
M R
MR
D049069:ATP-Dependent Proteases; D000255:Adenosine Triphosphate / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000201:enzymology; D015971:Gene Expression Regulation, Enzymologic; D006360:Heat-Shock Proteins / Q000378:metabolism*; D011387:Prokaryotic Cells / Q000201:enzymology; D012697:Serine Endopeptidases / Q000378:metabolism*
D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases