Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22
Abstract
We applied different methods (differential scanning calorimetry, circular dichroism, Fourier transform infrared spectroscopy, and intrinsic fluorescence) to investigate the thermal-induced changes in the structure of small heat shock protein Hsp22. It has been shown that this protein undergoes thermal-induced unfolding that occurs within a very broad temperature range (from 27 degrees C to 80 degrees C and above), and this is accompanied by complete disappearance of alpha-helices, significant decrease in beta-sheets content, and by pronounced changes in the intrinsic fluorescence. The results confirm predictions that Hsp22 belongs to the family of intrinsically disordered proteins (IDP) with certain parts of its molecule (presumably, in the alpha-crystallin domain) retaining folded structure and undergoing reversible thermal unfolding. The results are also discussed in terms of downhill folding scenario.
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IDPs are expected to have higher heat capacity than well-defined proteins, potentially 2-4 times that of globular proteins of equal mass.
“Proteins with very flexible conformations, such as intrinsically disordered proteins (IDP), are expected to have larger heat capacity than well-defined proteins.96–98”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [96]
Cites
Intrinsically unstructured proteins
Tompa, P. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02169-2 · Cited by 2,056 · see citing works
Natively unfolded proteins: A point where biology waits for physics
Uversky, V. N. (2002) · Protein Science · doi:10.1110/ps.4210102 · Cited by 1,815 · see citing works
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096 · see citing works
Energetics of Protein Structure
Makhatadze, G. I., & Privalov, P. L. (1995) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60548-3 · Cited by 1,073 · see citing works
What does it mean to be natively unfolded?
Uversky, V. N. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02649.x · Cited by 985 · see citing works
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847 · see citing works
Some like it hot: the structure and function of small heat-shock proteins
Haslbeck, M., Franzmann, T. M., Weinfurtner, D., & Büchner, J. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb993 · Cited by 830 · see citing works
[2]Scanning microcalorimetry in studying temperature-induced changes in proteins
Privalov, P. L., & Potekhin, S. A. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)31033-4 · Cited by 766 · see citing works
Experimental Identification of Downhill Protein Folding
García‐Mira, M. M., Sadqi, M., Fischer, N., Sánchez‐Ruiz, J. M., & Muñoz, V. (2002) · Science · doi:10.1126/science.1077809 · Cited by 307 · see citing works
sHsps and their role in the chaperone network
Haslbeck, M. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012492 · Cited by 293 · see citing works
Gusev, N. B., Bogatcheva, N. V., & Marston, S. B. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1015549725819 · Cited by 172 · see citing works
Self-citationWrapping the α-Crystallin Domain Fold in a Chaperone Assembly
Stamler, R., Kappé, G., Boelens, W. C., et al. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.025 · Cited by 142 · see citing works
Benndorf, R., Sun, X., Gilmont, R. R., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103001200 · Cited by 135 · see citing works
Goormaghtigh, E., Gasper, R., Bénard, A., Goldsztein, A., & Raussens, V. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.06.007 · Cited by 127 · see citing works
Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
Chowdary, T. K., Raman, B., Ramakrishna, T., et al. (2004) · Biochemical Journal · doi:10.1042/bj20031958 · Cited by 121 · see citing works
Some properties of human small heat shock protein Hsp20 (HspB6)
Bukach, O. V., Seit‐Nebi, A. S., Marston, S. B., & Gusev, N. B. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03928.x · Cited by 118 · see citing works
Self-citationUnfolding of a Leucine zipper is not a Simple Two-state Transition
Dragan, A. I., & Privalov, P. L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00699-x · Cited by 99 · see citing works
Ultra‐violet fluorescence of actin. Determination of native actin content in actin preparations
Turoverov, K. К., Haitlina, S. Y., & Pinaev, G. P. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80003-8 · Cited by 90 · see citing works
Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin
Pivovarova, A. V., Mikhaylova, V. V., Chernik, I. S., et al. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.077 · Cited by 87 · see citing works
Muñoz, V. (2002) · International Journal of Quantum Chemistry · doi:10.1002/qua.10384 · Cited by 81 · see citing works
Pivovarova, A. V., Chebotareva, N. A., Chernik, I. S., et al. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06117.x · Cited by 79 · see citing works
Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence
Permyakov, E. A., & Burstein, E. A. (1984) · Biophysical Chemistry · doi:10.1016/0301-4622(84)87009-x · Cited by 79 · see citing works
A new set of peptide-based group heat capacities for use in protein stability calculations
Häckel, M., Hinz, H., & Hedwig, G. R. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2952 · Cited by 71 · see citing works
Intrinsic Fluorescence of Actin
Turoverov, K. К., & Kuznetsova, I. М. (2003) · Journal of Fluorescence · doi:10.1023/a:1022366816812 · Cited by 69 · see citing works
Some properties of human small heat shock protein Hsp22 (H11 or HspB8)
Kim, M. V., Seit‐Nebi, A. S., Marston, S. B., & Gusev, N. B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.130 · Cited by 60 · see citing works
Self-citationShemetov, A. A., Seit‐Nebi, A. S., & Gusev, N. B. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21441 · Cited by 56 · see citing works
Self-citationApo‐parvalbumin as an intrinsically disordered protein
Permyakov, S. E., Bakunts, A. G., Denesyuk, A. I., Knyazeva, E. L., Uversky, V. N., & Permyakov, E. A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21974 · Cited by 56 · see citing works
Dimer structure as a minimum cooperative subunit of small heat-shock proteins
Dudich, I. V., Zav'yalov, V. P., Pfeil, W., et al. (1995) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(95)00135-x · Cited by 52 · see citing works
Khanova, H. A., Markossian, K. A., Kleimenov, S. Y., et al. (2006) · Biophysical Chemistry · doi:10.1016/j.bpc.2006.11.002 · Cited by 52 · see citing works
Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin
Panasenko, O. O., Kim, M. V., Marston, S. B., et al. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03449.x · Cited by 46 · see citing works
β-Tubulin Isotypes Purified from Bovine Brain Have Different Relative Stabilities
Schwarz, P. M., Liggins, J. R., & Ludueña, R. F. (1998) · Biochemistry · doi:10.1021/bi972763d · Cited by 43 · see citing works
Kim, M. V., Kasakov, A. S., Seit‐Nebi, A. S., et al. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.07.014 · Cited by 41 · see citing works
H11 has dose-dependent and dual hypertrophic and proapoptotic functions in cardiac myocytes
Hase, M., Depré, C., Vatner, S. F., & Sadoshima, J. (2005) · Biochemical Journal · doi:10.1042/bj20041314 · Cited by 41 · see citing works
Kremneva, E., Nikolaeva, O., Maytum, R., Arutyunyan, A. M., Kleimenov, S. Y., Geeves, M. A., & Levitsky, D. I. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05092.x · Cited by 40 · see citing works
Self-citationKasakov, A. S., Bukach, O. V., Seit‐Nebi, A. S., Marston, S. B., & Gusev, N. B. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06086.x · Cited by 34 · see citing works
Self-citationMarkov, D. I., Pivovarova, A. V., Chernik, I. S., et al. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.035 · Cited by 34 · see citing works
Self-citationA designed protein as experimental model of primordial folding
Sadqi, M., de Alba, E., Pérez‐Jiménez, R., Sánchez‐Ruiz, J. M., & Muñoz, V. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812108106 · Cited by 34 · see citing works
The conformational stability of α‐crystallin is rather low: Calorimetric results
Gesierich, U., & Pfeil, W. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00867-8 · Cited by 30 · see citing works
Staiano, M., Scognamiglio, V., Rossi, M., et al. (2005) · Biochemistry · doi:10.1021/bi0478300 · Cited by 28 · see citing works
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Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works
- Authors
- Kazakov, A. S., Markov, D. I., Gusev, N. B., & Levitsky, D. I.
- Affiliations
- Russian Academy of Sciences (RU)
- Lomonosov Moscow State University (RU)
- Corresponding author
- Levitsky, Dmitrii I.
- Venue
- Biophysical Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 145
- Issue
- 2-3
- Pages
- 79-85
- ISSN
- 0301-4622 (ISSN-L)
- OpenAlex
- W2109864603
- Cited by
- 43
- References
- 39
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 2 · 2018: 3 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 5 · 2012: 7
- FWCI
- 2.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biophysical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Russian Academy of Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- Hsp22, small heat shock proteins, intrinsically disordered proteins, thermal denaturation, protein folding, alpha-crystallin domain, downhill folding, alpha-helix content, β-sheet content, intrinsic fluorescence, protein structure
- MeSH terms
- Actins, Calorimetry, Differential Scanning, Hot Temperature, Heat-Shock Proteins, Humans, Mutation, Protein Binding, Protein Denaturation, Protein Serine-Threonine Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Molecular Chaperones, alpha-Crystallins
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