The effect of the dilated cardiomyopathy-causing mutation Glu54Lys of alpha-tropomyosin on actin-myosin interactions during the ATPase cycle.

Journal article

In order to understand how the Glu54Lys mutation of alpha-tropomyosin affects actomyosin interactions, we labeled SH1 helix of myosin subfragment-1 (S1) and the actin subdomain-1 with fluorescent probes. These proteins were incorporated into ghost muscle fibers and their conformational states were monitored during the ATPase cycle by measuring polarized fluorescence. The addition of wild-type alpha-tropomyosin to actin filaments increases the amplitude of the SH1 helix and subdomain-1 movemen...

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Authors: Borovikov, Y; Karpicheva, O; Avrova, S; Robinson, P; Redwood, C

• Publication status: Published
• Journal: Archives of biochemistry and biophysics
• Volume: 489
• Issue: 1-2
• Pages: 20-24
• Publication date: 2009-09-01
• DOI: 10.1016/j.abb.2009.07.018
• EISSN: 1096-0384
• ISSN: 0003-9861
• Language: English
• Keywords: Muscle Fibers, Skeletal; Protein Structure, Secondary; Cardiomyopathy, Dilated; Spectrometry, Fluorescence; Rabbits; Adenosine Triphosphatases; Animals; Tropomyosin; Mutation, Missense; Humans; Protein Structure, Tertiary; Amino Acid Substitution