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Article

The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8

by
Vladislav M. Shatov
1,
Stephen D. Weeks
2,
Sergei V. Strelkov
2 and
Nikolai B. Gusev
1,*
1
Department of Biochemistry, School of Biology, Moscow State University, Moscow 119991, Russia
2
Laboratory of Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Leuven 3000, Belgium
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(7), 2112; https://doi.org/10.3390/ijms19072112
Submission received: 17 June 2018 / Revised: 14 July 2018 / Accepted: 17 July 2018 / Published: 20 July 2018
(This article belongs to the Special Issue Molecular Chaperones)
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Abstract

Although the N-terminal domain of vertebrate small heat shock proteins (sHsp) is poorly conserved, it contains a core motif preserved in many members of the sHsp family. The role of this RLFDQxFG motif remains elusive. We analyzed the specific role of the first arginine residue of this conserved octet sequence in five human sHsps (HspB1, HspB4, HspB5, HspB6, and HspB8). Substitution of this arginine with an alanine induced changes in thermal stability and/or intrinsic fluorescence of the related HspB1 and HspB8, but yielded only modest changes in the same biophysical properties of HspB4, HspB5, and HspB6 which together belong to another clade of vertebrate sHsps. Removal of the positively charged Arg side chain resulted in destabilization of the large oligomers of HspB1 and formation of smaller size oligomers of HspB5. The mutation induced only minor changes in the structure of HspB4 and HspB6. In contrast, the mutation in HspB8 was accompanied by shifting the equilibrium from dimers towards the formation of larger oligomers. We conclude that the RLFDQxFG motif plays distinct roles in the structure of several sHsp orthologs. This role correlates with the evolutionary relationship of the respective sHsps, but ultimately, it reflects the sequence context of this motif.
Keywords: small heat shock proteins; oligomer structure; chaperone-like activity; disease-related mutations small heat shock proteins; oligomer structure; chaperone-like activity; disease-related mutations
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MDPI and ACS Style

Shatov, V.M.; Weeks, S.D.; Strelkov, S.V.; Gusev, N.B. The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8. Int. J. Mol. Sci. 2018, 19, 2112. https://doi.org/10.3390/ijms19072112

AMA Style

Shatov VM, Weeks SD, Strelkov SV, Gusev NB. The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8. International Journal of Molecular Sciences. 2018; 19(7):2112. https://doi.org/10.3390/ijms19072112

Chicago/Turabian Style

Shatov, Vladislav M., Stephen D. Weeks, Sergei V. Strelkov, and Nikolai B. Gusev. 2018. "The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8" International Journal of Molecular Sciences 19, no. 7: 2112. https://doi.org/10.3390/ijms19072112

APA Style

Shatov, V. M., Weeks, S. D., Strelkov, S. V., & Gusev, N. B. (2018). The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8. International Journal of Molecular Sciences, 19(7), 2112. https://doi.org/10.3390/ijms19072112

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