Molecular mechanisms of deregulation of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1

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• 作者：Yurii S. Borovikov^a ; ^{borovikov@incras.ru} ; Nikita A. Rysev^a ; Stanislava V. Avrova^a ; Olga E. Karpicheva^a ; Danuta Borys^b ; Joanna Moraczewska^b
• 关键词：Tropomyosin ; F-actin ; Myosin ; Troponin ; Ghost muscle fibres ; Congenital myopathies ; Fluorescence polarization
• 刊名：Archives of Biochemistry and Biophysics
• 出版年：2017
• 出版时间：15 January 2017
• 年：2017
• 卷：614
• 期：Complete
• 页码：28-40
• 全文大小：2334 K
• 卷排序：614

文摘

R167H and K168E mutations in TPM1 affect conformation of the thin filament. Mutant tropomyosin, actin and myosin heads move abnormally both at low and high Са2+. R167H substitution enhances Cа2+-sensitivity at low Са2+ and inhibits strong-binding state at high Са2+. K168E substitution increases fraction of rigor myosin heads at low Са2+ and reduces it at high Са2+. The mutations change thin filament regulation through different mechanisms.