structural sudies of ClpS, dem RpoS/RssB-Target System und FtsH

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Protein synthesis and degradation in the bacterial cell is tightly controlled by a number of molecular chaperones and proteases. Particularly important are the ClpAP and ClpXP protease complexes, which are specific targets of misfolded cytosolic and short-lived polypeptides, whereas the FtsH protease acts primarily on integral membrane proteins. ClpAP and ClpXP are ATP-dependent, processive proteases composed of a ClpP proteolytic subunit and either a ClpA or ClpX chaperone belonging to the AAA family of ATPases while FtsH combines both functions within one polypeptide chain. There are a few proteins known which play a role as substrate sensors for ClpXP and ClpAP. The substrate sensory protein ClpS for instance enhances the substrate specificity of the ClpAP protease and the response regulator RssB specifically targets the rpos-encoded sS factor for ClpXP-mediated degradation.