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Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine
Open accessAbstract
All cells employ ATP-powered proteases for protein-quality control and regulation. In the ClpXP protease, ClpX is a AAA+ machine that recognizes specific protein substrates, unfolds these molecules, and then translocates the denatured polypeptide through a central pore and into ClpP for degradation. Here, we use optical-trapping nanometry to probe the mechanics of enzymatic unfolding and translocation of single molecules of a multidomain substrate. Our experiments demonstrate the capacity of ClpXP and ClpX to perform mechanical work under load, reveal very fast and highly cooperative unfolding of individual substrate domains, suggest a translocation step size of 5–8 amino acids, and support a power-stroke model of denaturation in which successful enzyme-mediated unfolding of stable domains requires coincidence between mechanical pulling by the enzyme and a transient stochastic reduction in protein stability. We anticipate that single-molecule studies of the mechanical properties of other AAA+ proteolytic machines will reveal many shared features with ClpXP.
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Direct observation of kinesin stepping by optical trapping interferometry
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Targeting proteins for degradation.
Schrader, E. K., Harstad, K. G., & Matouschek, A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.250 · Cited by 287
Cited by
Complete subunit architecture of the proteasome regulatory particle
Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Ribas-Arino, J., & Marx, D. (2012) · Chemical Reviews · doi:10.1021/cr200399q · Cited by 448
Conformational switching of the 26S proteasome enables substrate degradation
Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2616 · Cited by 251
Regulated protein turnover: snapshots of the proteasome in action
Bhattacharyya, S., Yu, H., Mim, C., & Matouschek, A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3741 · Cited by 240
Metadata
- Authors
- Aubin-Tam, M.-E., Olivares, A. O., Sauer, R. T., Baker, T. A., & Lang, M. J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 145
- Issue
- 2
- Pages
- 257-267
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2046105451
- Cited by
- 294
- References
- 2
- FWCI
- 10.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Aubin-Tam, M.-E., Olivares, A. O., Sauer, R. T., Baker, T. A., & Lang, M. J. (2011). Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine. Cell. https://doi.org/10.1016/j.cell.2011.03.036
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