Abstract：
: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 analyses reveal that phosphate release is the force-generating step in the ATP-hydrolysis cycle and that ClpXP translocates substrate polypeptides in bursts resulting from highly coordinated conformational changes in two to four ATPase subunits. ClpXP must use its maximum successive firing capacity of four subunits to unfold stable substrates like GFP. The average dwell duration between individual bursts of translocation is constant, regardless of the number of translocating subunits, implying that ClpXP operates with constant "rpm" but uses different "gears."
journal_name
Celljournal_title
Cellauthors
Sen M,Maillard RA,Nyquist K,Rodriguez-Aliaga P,Pressé S,Martin A,Bustamante Cdoi
10.1016/j.cell.2013.09.022subject
Has Abstractpub_date
2013-10-24 00:00:00pages
636-646issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(13)01159-8journal_volume
155pub_type
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