Book contents
- Frontmatter
- Contents
- Contributors
- Figures and Tables
- Preface
- Introduction
- Chapter 1 Single-Molecule FRET: Technique and Applications to the Studies of Molecular Machines
- Chapter 2 Visualization of Molecular Machines by Cryo-Electron Microscopy
- Chapter 3 Statistical Mechanical Treatment of Molecular Machines
- Chapter 4 Exploring the Functional Landscape of Biomolecular Machines via Elastic Network Normal Mode Analysis
- Chapter 5 Structure, Function, and Evolution of Archaeo-Eukaryotic RNA Polymerases – Gatekeepers of the Genome
- Chapter 6 Single-Molecule Fluorescence Resonance Energy Transfer Investigations of Ribosome-Catalyzed Protein Synthesis
- Chapter 7 Structure and Dynamics of the Ribosome as Revealed by Cryo-Electron Microscopy
- Chapter 8 Viewing the Mechanisms of Translation through the Computational Microscope
- Chapter 9 The Ribosome as a Brownian Ratchet Machine
- Chapter 10 The GroEL/GroES Chaperonin Machine
- Chapter 11 ATP Synthase – A Paradigmatic Molecular Machine
- Chapter 12 ATP-Dependent Proteases: The Cell's Degradation Machines
- Index
- References
Chapter 12 - ATP-Dependent Proteases: The Cell's Degradation Machines
Published online by Cambridge University Press: 05 January 2012
Book contents
- Frontmatter
- Contents
- Contributors
- Figures and Tables
- Preface
- Introduction
- Chapter 1 Single-Molecule FRET: Technique and Applications to the Studies of Molecular Machines
- Chapter 2 Visualization of Molecular Machines by Cryo-Electron Microscopy
- Chapter 3 Statistical Mechanical Treatment of Molecular Machines
- Chapter 4 Exploring the Functional Landscape of Biomolecular Machines via Elastic Network Normal Mode Analysis
- Chapter 5 Structure, Function, and Evolution of Archaeo-Eukaryotic RNA Polymerases – Gatekeepers of the Genome
- Chapter 6 Single-Molecule Fluorescence Resonance Energy Transfer Investigations of Ribosome-Catalyzed Protein Synthesis
- Chapter 7 Structure and Dynamics of the Ribosome as Revealed by Cryo-Electron Microscopy
- Chapter 8 Viewing the Mechanisms of Translation through the Computational Microscope
- Chapter 9 The Ribosome as a Brownian Ratchet Machine
- Chapter 10 The GroEL/GroES Chaperonin Machine
- Chapter 11 ATP Synthase – A Paradigmatic Molecular Machine
- Chapter 12 ATP-Dependent Proteases: The Cell's Degradation Machines
- Index
- References
Summary
Introduction
Protein concentration in the cell is a function of the rates of protein synthesis and destruction, and the regulation of both processes is necessary for a properly functioning cell. The degradation of proteins is mainly performed by a small number of ATP-dependent cellular proteases. ATP-dependent proteases are molecular motors that degrade substrates by translocating along the substrates’ polypeptide chain. Degradation is directional, highly processive, and requires energy from ATP hydrolysis (Kim et al., 2000; Lee et al., 2001; Reid et al., 2001; Kenniston et al., 2003; Aubin-Tam et al., 2011; Maillard et al., 2011). In this manner, these proteases control the concentrations of hundreds of regulatory proteins involved in processes such as the cell cycle, transcription, and signal transduction and play an important housekeeping role by destroying misfolded and damaged proteins (Ciechanover, 1994; Glickman and Ciechanover, 2002; Goldberg, 2003; Collins and Tansey, 2006). Despite this wide range of substrates, proteases have to act specifically to avoid the unintended degradation of the rest of the cellular proteins. ATP-dependent proteases in Bacteria, Archaea, and Eukaryotes have evolved a similar way of solving this problem: their proteolytic sites are encapsulated within the protease structure where they are inaccessible to folded proteins (Baumeister et al., 1998). Substrates are targeted to the proteases via specific degradation signals, to be unraveled and translocated into the proteolytic chamber (Baker and Sauer, 2006; Schrader et al., 2009). The unfolding and translocation of substrates is accelerated by ATP hydrolysis and is catalyzed by ATPase domains or subunits that flank the proteolytic barrel and pull at the substrates’ polypeptide chains (Prakash and Matouschek, 2004, Sauer et al., 2004; Aubin-Tam et al., 2011; Maillard et al., 2011). In this chapter, we will introduce the main ATP-dependent proteases in Bacteria, Archaea, and Eukaryotes and attempt to describe the common mechanisms through which they recognize and degrade their substrates.
- Type
- Chapter
- Information
- Molecular Machines in BiologyWorkshop of the Cell, pp. 239 - 260Publisher: Cambridge University PressPrint publication year: 2011
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