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Myopathic mutations in the β‐chain of tropomyosin differently affect the structural and functional properties of ββ‐ and αβ‐dimers
Author(s) -
Bershitsky Sergey Y.,
Logvinova Daria S.,
Shchepkin Daniil V.,
Kopylova Galina V.,
Matyushenko Alexander M.
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.201800755r
Subject(s) - tropomyosin , affect (linguistics) , chemistry , chain (unit) , genetics , biology , biochemistry , actin , psychology , communication , physics , astronomy
Tropomyosin (Tpm) is an actin‐binding protein that plays a vital role in the regulation of muscle contraction. Fast skeletal muscles express 2 Tpm isoforms, α (Tpm 1.1) and β (Tpm 2.2), resulting in the existence of 2 forms of dimeric Tpm molecule: αα‐homodimer and αβ‐heterodimer. ββ‐Homodimer is unstable and absent in the native state, despite which most of the studies of myopathy‐relating Tpm mutations have been performed on the ββ‐homodimer. Here, we applied different methods to investigate the effects of myopathic mutations R133W and N202K in the β‐chain of Tpm on properties of αβ‐heterodimers and to compare them with the features of ββ‐homodimers with the same mutations. The results show that properties of αβ‐Tpm and ββ‐Tpm with substitutions in the β‐chain differ significantly, and this indicates that the effects of myopathic mutations in the Tpm β‐chain should be studied on the Tpm αβ‐heterodimer.—Bershitsky, S. Y., Logvinova, D. S., Shchepkin, D. V., Kopylova, G. V., Matyushenko, A. M. Myopathic mutations in the β‐chain of tropomyosin differently affect the structural and functional properties of ββ‐ and αβ‐dimers. FASEB J. 33, 1963–1971 (2019). www.fasebj.org