Unlike many eukaryotic proteasomes, which have several different peptide substrate specificities, hslV has a specificity similar to that of chymotrypsin hence it is inhibited by proteasome inhibitors that specifically target the chymotrypsin site in eukaryotic proteasomes. īoth proteins are encoded on the same operon within the bacterial genome. HslV bears high similarity to core subunits of proteasomes. HslV is thought to resemble the hypothetical ancestor of the proteasome, a large protein complex specialized for regulated degradation of unneeded proteins in eukaryotes, many archaea, and a few bacteria. The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. The hslV protein is a protease and the hslU protein is an ATPase the two form a symmetric assembly of four stacked rings, consisting of an hslV dodecamer bound to an hslU hexamer, with a central pore in which the protease and ATPase active sites reside.
The heat shock proteins HslV and HslU ( HslVU complex also known as ClpQ and ClpY respectively, or ClpQY) are expressed in many bacteria such as E. Top view of the hslV/hslU complex isolated from E.
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