The ClpXP Protease Unfolds Substrates Using a Constant Rate of Pulling but Different Gears

ATP-dependent proteases are vital to maintain cellular protein homeostasis. Here, we study the mechanisms of force generation and intersubunit coordination in the ClpXP protease from E. coli to understand how these machines couple ATP hydrolysis to mechanical protein unfolding. Single-molecule analy...

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Veröffentlicht in:	Cell 2013-10, Vol.155 (3), p.636-646
Hauptverfasser:	Sen, Maya, Maillard, Rodrigo A., Nyquist, Kristofor, Rodriguez-Aliaga, Piere, Pressé, Steve, Martin, Andreas, Bustamante, Carlos
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism adenosine triphosphate Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism adenosinetriphosphatase Endopeptidase Clp - chemistry Endopeptidase Clp - metabolism Escherichia coli Escherichia coli - enzymology Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism homeostasis hydrolysis Optical Tweezers phosphates Phosphates - metabolism polypeptides proteases Protein Conformation Protein Subunits - chemistry Protein Subunits - metabolism Protein Unfolding proteinases
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