The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates
Open accessAbstract
SUMMARY AAA+ unfoldases denature and translocate polypeptides into associated peptidases. We report direct observations of mechanical, force-induced protein unfolding by the ClpX unfoldase from E. coli, alone, and in complex with the ClpP peptidase. ClpX hydrolyzes ATP to generate mechanical force and translocate polypeptides through its central pore. Threading is interrupted by pauses that are found to be off the main translocation pathway. ClpX’s translocation velocity is force dependent, reaching a maximum of 80 aa/s near-zero force and vanishing at around 20 pN. ClpX takes 1, 2, or 3 nm steps, suggesting a fundamental step-size of 1 nm and a certain degree of intersubunit coordination. When ClpX encounters a folded protein, it either overcomes this mechanical barrier or slips on the polypeptide before making another unfolding attempt. Binding of ClpP decreases the slip probability and enhances the unfolding efficiency of ClpX. Under the action of ClpXP, GFP unravels cooperatively via a transient intermediate.
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Crystal Structure of the Aequorea victoria Green Fluorescent Protein
Ormö, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., & Remington, S. J. (1996) · Science · doi:10.1126/science.273.5280.1392 · Cited by 2,242
Entropic Elasticity of λ-Phage DNA
Bustamante, C., Marko, J. F., Siggia, E. D., & Smith, S. (1994) · Science · doi:10.1126/science.8079175 · Cited by 2,154
Self-citationDirect observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
The molecular structure of green fluorescent protein
Yang, F., Moss, L. G., & Phillips, G. N. (1996) · Nature Biotechnology · doi:10.1038/nbt1096-1246 · Cited by 1,576
Thermodynamics and Kinetics of a Brownian Motor
Astumian, R. D. (1997) · Science · doi:10.1126/science.276.5314.917 · Cited by 1,411
How Proteolysis Drives the Cell Cycle
King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273
The bacteriophage φ29 portal motor can package DNA against a large internal force
Smith, D. E., Tans, S. J., Smith, S. B., Grimes, S., Anderson, D. L., & Bustamante, C. (2001) · Nature · doi:10.1038/35099581 · Cited by 1,032
Self-citationIonic effects on the elasticity of single DNA molecules
Baumann, C. G., Smith, S. B., Bloomfield, V. A., & Bustamante, C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6185 · Cited by 1,001
Self-citationDirect observation of base-pair stepping by RNA polymerase
Abbondanzieri, E. A., Greenleaf, W. J., Shaevitz, J. W., Landick, R., & Block, S. M. (2005) · Nature · doi:10.1038/nature04268 · Cited by 855
Gottesman, S., Roche, E., Zhou, Y., & Sauer, R. T. (1998) · Genes & Development · doi:10.1101/gad.12.9.1338 · Cited by 835
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Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608
Self-citationWei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
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Metadata
- Authors
- Maillard, R. A., Chistol, G., Sen, M., Righini, M., Tan, J., Kaiser, C. M., Hodges, C., Martin, A., & Bustamante, C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 145
- Issue
- 3
- Pages
- 459-469
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2113681346
- Cited by
- 286
- References
- 36
- FWCI
- 9.87
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Maillard, R. A., Chistol, G., Sen, M., Righini, M., Tan, J., Kaiser, C. M., Hodges, C., Martin, A., & Bustamante, C. (2011). ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates. Cell. https://doi.org/10.1016/j.cell.2011.04.010
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