Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon.

作者: S. Wickner , M. R. Maurizi

DOI: 10.1073/PNAS.96.15.8318

关键词: Protein foldingBiologyProtein structureCo-chaperoneChaperone (protein)BiochemistryProteasesPlasma protein bindingHeat shock proteinATP-Dependent Proteases

摘要: Protein quality control mechanisms are essential to ensure the proper levels of functional proteins within cell and eliminate nonfunctional from cell. To this end, maintains an array molecular chaperones help fold into their native conformations, prevent aggregation, assist in assembly multiprotein complexes, along with ATP-dependent proteases degrade damaged or improperly synthesized (reviewed refs. 1–4). Also, intracellular concentrations activities a limited number normal cellular modulated by these same chaperones. These natural protein targets often key regulatory involved vital processes such as division, stress responses, developmental changes. avoid potentially lethal damage inappropriate components, have evolved rather complex energy-dependent assure accurate substrate recognition.

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