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• W1564184132 abstract "Publisher Summary This chapter reviews recent data obtained with Escherichia coli adenosine triphosphate (ATP)-dependent proteases that suggest that chaperones and proteases are partners in a system of protein-quality control, and that the ability of a targeted protein to either adopt a stable conformation or assemble into a macromolecular complex is probably a major determinant of whether it is refolded or degraded. The regulatory functions of protein degradation involve essentially every vital process in the cell, because many of the rapidly degraded proteins are themselves important regulatory proteins, including transcription factors, replication proteins, cell-division inhibitors, and other proteins involved in multimeric, multifunctional-enzyme complexes. Thus, in different organisms, protein degradation is involved in the timing of cell division, heat shock, and other stress responses, DNA repair and mutagenesis, developmental changes, and response to nutrient depletion. The chapter describes some of the biological functions of proteases in bacterial cells. Protein degradation also serves in protein quality control, an important role often classified as a housekeeping function." @default.
• W1564184132 created "2016-06-24" @default.
• W1564184132 creator A5087235422 @default.
• W1564184132 date "1998-01-01" @default.
• W1564184132 modified "2023-09-25" @default.
• W1564184132 title "Biochemical Properties and Biological Functions of Atp-Dependent Proteases In Bacterial Cells" @default.
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