ClpX shifts into high gear to unfold stable proteins.
Protein degradation by the ClpXP protease requires collaboration among the six AAA+ domains of ClpX. Using single-molecule optical tweezers, Sen et al. show that ClpX uses a coordinated succession of power strokes to translocate polypeptides in ATP-tunable bursts before reloading with nucleotide. This strategy allows ClpX to kinetically capture transiently unfolded intermediates.
Laboratory of Cell Biology, National Cancer Institute, Bethesda, MD 20892, USA. Electronic address: mmaurizi@helix.nih.gov.
Michael R
MR
Maurizi
George
G
Stan
D049071:Endopeptidase Clp / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*
D029968:Escherichia coli Proteins; C483573:ClpXP protease, E coli; D049071:Endopeptidase Clp