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Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin
Open accessAbstract
The quaternary structure of the polydisperse mammalian chaperone αB-crystallin, a member of the small heat-shock protein family, has been investigated by using electrospray mass spectrometry. The intact assemblies give rise to mass spectra that are complicated by the overlapping of charge states from the different constituent oligomers. Therefore, to determine which oligomers are formed by this protein, tandem mass spectrometry experiments were performed. The spectra reveal a distribution, primarily of oligomers containing 24–33 subunits, the relative populations of which were quantified, to reveal a dominant species being composed of 28 subunits. Additionally, low levels of oligomers as small as 10-mers and as large as 40-mers were observed. Interpretation of the tandem mass spectral data was confirmed by simulating and summing spectra arising from the major individual oligomers. The ability of mass spectrometry to quantify the relative populations of particular oligomeric states also revealed that, contrary to the dimeric associations observed in other small heat-shock proteins, there is no evidence for any stable substructures of bovine αB-crystallin isolated from the lens.
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Cited by
Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000
Self-citationAgeing and vision: structure, stability and function of lens crystallins
Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N. H., Slingsby, C., & Tardieu, A. (2004) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2003.11.012 · Cited by 853
Self-citationProtein Complexes in the Gas Phase: Technology for Structural Genomics and Proteomics
Benesch, J. L. P., Ruotolo, B. T., Simmons, D. A., & Robinson, C. V. (2007) · Chemical Reviews · doi:10.1021/cr068289b · Cited by 408
Self-citationThe Role of Mass Spectrometry in Structure Elucidation of Dynamic Protein Complexes
Sharon, M., & Robinson, C. V. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.090816 · Cited by 357
Self-citationOne size does not fit all: The oligomeric states of αB crystallin
Delbecq, S. P., & Klevit, R. E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.021 · Cited by 263
Metadata
- Authors
- Aquilina, J. A., Benesch, J. L. P., Bateman, O. A., Slingsby, C., & Robinson, C. V.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-08-28
- Volume
- 100
- Issue
- 19
- Pages
- 10611-10616
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2156628627
- Cited by
- 243
- References
- 0
- FWCI
- 4.18
- Type
- journal article
- Language
- en
- Open access
- green
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- Aquilina, J. A., Benesch, J. L. P., Bateman, O. A., Slingsby, C., & Robinson, C. V. (2003). Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1932958100
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