Effect of Disulfide Crosslinking on Thermal Transitions and Chaperone-like Activity of Human Small Heat Shock Protein HspB1

Overview

Journal Cell Stress Chaperones

Publisher Elsevier

Specialty Cell Biology

Date 2014 Jun 6

PMID 24898092

Citations 13

Authors

Anna S Chalova

Maria V Sudnitsyna

Pavel I Semenyuk

Victor N Orlov

Nikolai B Gusev

Affiliations

Soon will be listed here.

Abstract

Temperature-induced conformational changes of reduced and oxidized HspB1 crosslinked by disulfide bond between single Cys137 of neighboring monomers were analyzed by means of different techniques. Heating of reduced HspB1 was accompanied by irreversible changes of Trp fluorescence, whereas oxidized HspB1 underwent completely reversible changes of fluorescence. Increase of the temperature in the range of 20-70 °C was accompanied by self-association of both reduced and oxidized protein. Further increase of the temperature led to formation of heterogeneous mixture of large self-associated complexes of reduced HspB1 and to formation of smaller and less heterogeneous complexes of oxidized HspB1. Heat-induced changes of oligomeric state of reduced HspB1 were only partially reversible, whereas the corresponding changes of oligomeric state of oxidized HspB1 were almost completely reversible. Oxidation resulted in decrease of chaperone-like activity of HspB1. It is concluded that oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1.

Citing Articles

Key Role of Phosphorylation in Small Heat Shock Protein Regulation via Oligomeric Disaggregation and Functional Activation.

Sluzala Z, Hamati A, Fort P Cells. 2025; 14(2).

PMID: 39851555 PMC: 11764305. DOI: 10.3390/cells14020127.

Homo-oxidized HSPB1 protects H9c2 cells against oxidative stress via activation of KEAP1/NRF2 signaling pathway.

Wang N, Liu X, Liu K, Wang K, Zhang H iScience. 2023; 26(8):107443.

PMID: 37575200 PMC: 10415933. DOI: 10.1016/j.isci.2023.107443.

Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.

Tedesco B, Cristofani R, Ferrari V, Cozzi M, Rusmini P, Casarotto E Front Mol Biosci. 2022; 9:842149.

PMID: 35281256 PMC: 8913478. DOI: 10.3389/fmolb.2022.842149.

Oligomeric Structural Transition of HspB1 from Chinese Hamster.

Kurokawa N, Midorikawa R, Nakamura M, Noguchi K, Morishima K, Inoue R Int J Mol Sci. 2021; 22(19).

PMID: 34639138 PMC: 8509488. DOI: 10.3390/ijms221910797.

Bmal1 Regulates the Redox Rhythm of HSPB1, and Homooxidized HSPB1 Attenuates the Oxidative Stress Injury of Cardiomyocytes.

Liu X, Xiao W, Jiang Y, Zou L, Chen F, Xiao W Oxid Med Cell Longev. 2021; 2021:5542815.

PMID: 34239687 PMC: 8238613. DOI: 10.1155/2021/5542815.

References

Kriehuber T, Rattei T, Weinmaier T, Bepperling A, Haslbeck M, Buchner J . Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J. 2010; 24(10):3633-42. DOI: 10.1096/fj.10-156992. View

Eaton P, Byers H, Leeds N, Ward M, Shattock M . Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem. 2002; 277(12):9806-11. DOI: 10.1074/jbc.M111454200. View

Eaton P, Fuller W, Shattock M . S-thiolation of HSP27 regulates its multimeric aggregate size independently of phosphorylation. J Biol Chem. 2002; 277(24):21189-96. DOI: 10.1074/jbc.M200591200. View

Hochberg G, Benesch J . Dynamical structure of αB-crystallin. Prog Biophys Mol Biol. 2014; 115(1):11-20. DOI: 10.1016/j.pbiomolbio.2014.03.003. View

Bushueva T, Busel E, Burstein E . Some regularities of dynamic accessibility of buried fluorescent residues to external quenchers in proteins. Arch Biochem Biophys. 1980; 204(1):161-6. DOI: 10.1016/0003-9861(80)90019-3. View

Aquilina J, Benesch J, Ding L, Yaron O, Horwitz J, Robinson C . Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure. J Biol Chem. 2004; 279(27):28675-80. DOI: 10.1074/jbc.M403348200. View

Lelj-Garolla B, Mauk A . Roles of the N- and C-terminal sequences in Hsp27 self-association and chaperone activity. Protein Sci. 2011; 21(1):122-33. PMC: 3323787. DOI: 10.1002/pro.761. View

Skouri-Panet F, Quevillon-Cheruel S, Michiel M, Tardieu A, Finet S . sHSPs under temperature and pressure: the opposite behaviour of lens alpha-crystallins and yeast HSP26. Biochim Biophys Acta. 2006; 1764(3):372-83. DOI: 10.1016/j.bbapap.2005.12.011. View

Christians E, Ishiwata T, Benjamin I . Small heat shock proteins in redox metabolism: implications for cardiovascular diseases. Int J Biochem Cell Biol. 2012; 44(10):1632-45. PMC: 3412898. DOI: 10.1016/j.biocel.2012.06.006. View

10.

Weeds A, Taylor R . Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature. 1975; 257(5521):54-6. DOI: 10.1038/257054a0. View

11.

Mchaourab H, Godar J, Stewart P . Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins. Biochemistry. 2009; 48(18):3828-37. PMC: 2785012. DOI: 10.1021/bi900212j. View

12.

Zavialov A, Benndorf R, Ehrnsperger M, Zavyalov V, Dudich I, Buchner J . The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. Int J Biol Macromol. 1998; 22(3-4):163-73. DOI: 10.1016/s0141-8130(98)00014-2. View

13.

Diaz-Latoud C, Buache E, Javouhey E, Arrigo A . Substitution of the unique cysteine residue of murine Hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation. Antioxid Redox Signal. 2005; 7(3-4):436-45. DOI: 10.1089/ars.2005.7.436. View

14.

Ehrnsperger M, Lilie H, Gaestel M, Buchner J . The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species. J Biol Chem. 1999; 274(21):14867-74. DOI: 10.1074/jbc.274.21.14867. View

15.

Arrigo A . The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis. Adv Exp Med Biol. 2007; 594:14-26. DOI: 10.1007/978-0-387-39975-1_2. View

16.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

17.

Taylor R, Benjamin I . Small heat shock proteins: a new classification scheme in mammals. J Mol Cell Cardiol. 2005; 38(3):433-44. DOI: 10.1016/j.yjmcc.2004.12.014. View

18.

Pasupuleti N, Gangadhariah M, Padmanabha S, Santhoshkumar P, Nagaraj R . The role of the cysteine residue in the chaperone and anti-apoptotic functions of human Hsp27. J Cell Biochem. 2010; 110(2):408-19. PMC: 4562675. DOI: 10.1002/jcb.22552. View

19.

Mymrikov E, Bukach O, Seit-Nebi A, Gusev N . The pivotal role of the beta 7 strand in the intersubunit contacts of different human small heat shock proteins. Cell Stress Chaperones. 2009; 15(4):365-77. PMC: 3082641. DOI: 10.1007/s12192-009-0151-8. View

20.

Arrigo A . Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update. FEBS Lett. 2013; 587(13):1959-69. DOI: 10.1016/j.febslet.2013.05.011. View