The Effect of Stabilizing Mutations in the Central Part of α-Chain of Tropomyosin on the Bending Stiffness of Reconstructed Thin ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-01

AUTHORS

S. R. Nabiev, L. V. Nikitina, O. P. Hertsen, A. M. Matyushenko, D. V. Shchepkin, G. V. Kopylova, S. Y. Bershitsky, A. K. Tsaturyan, D. I. Levitsky

ABSTRACT

We studied the effect of the replacement of two highly conserved noncanonical residues in the α-chain of tropomyosin, that is, Asp137 and Gly126, with the canonical residues, Leu and Arg, on the mechanical properties of reconstructed thin filaments that contain αβ-heterodimers of tropomyosin. For this purpose, the reconstructed thin filaments that contain fibrillar actin, tropomyosin, and troponin were stretched with an optical trap. The resulting strain–force diagrams were analyzed using a mathematical model proposed previously in order to estimate the bending stiffness. It was shown that the thin filaments that contain αβ-heterodimers of tropomyosin with α-chains of the pseudo-wild type, i.e., that contain the C190A substitution, have approximately the same bending stiffness as the filament with αα-homodimers of tropomyosin. The stabilizing substitution D137L in the α-chain of tropomyosin did not cause a statistically significant change in the bending stiffness of the filaments that contain αβ-heterodimers of tropomyosin, whereas the G126R and G126R/D137L substitutions led to a moderate increase in this stiffness. This increase in stiffness was, however, much less pronounced than that for the filaments that contain αα-homodimers of tropomyosin with these substitutions in both α-chains. The relationship between the results obtained in this study and the previously published data on the effects of these stabilizing substitutions in the α-chain of tropomyosin on the structural and functional properties of thin filaments with αβ-heterodimers of tropomyosin is discussed. More... »

PAGES

20-24

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0006350918010116

DOI

http://dx.doi.org/10.1134/s0006350918010116

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1103608918


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