Cell, 1997, Vol.91(4), pp.435-438
Much of our current knowledge about specific steps in energy-dependent degradation and the role of accessory factors comes from studies of the prokaryotic ATP-dependent proteases, ClpAP and ClpXP, which are complexes of separately encoded ATPase and peptidase subunits, and the homomeric Lon and FtsH proteases, in which both functions are encoded within single polypeptide chains. We would like to propose that the similarity in structure between the ClpAP or ClpXP proteases and the 26S proteasome, despite their apparent evolutionary unrelatedness, reflects underlying similarities in the biochemical mechanism of protein degradation. The existence of ClpYQ (HslUV), a hybrid between a protease homologous to the proteasome and a Clp ATPase, reinforces this suggestion.
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