There are five known ATP-dependent proteases in Escherichia coli (Lon, ClpAP, ClpXP,
HslUV, and the membrane-associated FtsH) that catalyze the removal of both misfolded and …

The removal of damaged or unneeded proteins by ATP-dependent proteases is crucial for
cell survival in all organisms. Integral components of ATP-dependent proteases are motor …

Escherichia coli caseinolytic protease (Clp) B is a hexameric AAA+ [expanded superfamily
of AAA (ATPase associated with various cellular activities)] enzyme that has the unique …

Escherichia coli ClpA and ClpX are ATP-dependent protein unfoldases that each interact
with the protease, ClpP, to promote specific protein degradation. We have used limited …

Enzyme-catalyzed protein unfolding is essential for a large array of biological functions,
including microtubule severing, membrane fusion, morphogenesis and trafficking of …

The Escherichia coli ATP-dependent protease, ClpAP, is composed of the hexameric
ATPase/protein-unfoldase, ClpA, and the tetradecameric proteolytic component, ClpP. ClpP …

The Escherichia coli ClpA and ClpP proteins form a complex, ClpAP, that catalyzes ATP-
dependent degradation of proteins. Formation of stable ClpA hexamers and stable ClpAP …

Abstract The Escherichia coli ClpA protein is a molecular chaperone that binds and
translocates protein substrates into the proteolytic cavity of the tetradecameric serine …

Proteolysis functions as a precise regulatory mechanism for a broad spectrum of cellular
processes. Such control impacts not only on the stability of key metabolic enzymes but also …

Clp is a barrel-shaped hetero-oligomeric ATP-dependent protease comprising a hexameric
ATPase (ClpX or ClpA) that unfolds protein substrates and translocates them into the central …