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Ligand-Dependent Equilibrium Fluctuations of Single Calmodulin Molecules
Abstract
Single-molecule force spectroscopy allows superb mechanical control of protein conformation. We used a custom-built low-drift atomic force microscope to observe mechanically induced conformational equilibrium fluctuations of single molecules of the eukaryotic calcium-dependent signal transducer calmodulin (CaM). From this data, the ligand dependence of the full energy landscape can be reconstructed. We find that calcium ions affect the folding kinetics of the individual CaM domains, whereas target peptides stabilize the already folded structure. Single-molecule data of full length CaM reveal that a wasp venom peptide binds noncooperatively to CaM with 2:1 stoichiometry, whereas a target enzyme peptide binds cooperatively with 1:1 stoichiometry. If mechanical load is applied directly to the target peptide, real-time binding/unbinding transitions can be observed.
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Citations
Cited by
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Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008
Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Force-dependent conformational switch of α-catenin controls vinculin binding
Yao, M., Qiu, W., Liu, R., Efremov, A. K., Cong, P., Seddiki, R., Payre, M., Lim, C. T., Ladoux, B., Mège, R.-M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5525 · Cited by 454
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Gao, Y., Zorman, S., Gundersen, G., Xi, Z., Ma, L., Sirinakis, G., Rothman, J. E., & Zhang, Y. (2012) · Science · doi:10.1126/science.1224492 · Cited by 405
Metadata
- Authors
- Junker, J. P., Ziegler, F., & Rief, M.
- Venue
- Science
- Published
- 2009-01-30
- Volume
- 323
- Issue
- 5914
- Pages
- 633-637
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1986156047
- Cited by
- 211
- References
- 0
- FWCI
- 16.17
- Type
- journal article
- Language
- en
- Open access
- closed
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