Abstract:
:The effect of the skeletal myopathy-causing E117K mutation in human β-tropomyosin on actomyosin structure during the ATPase cycle was studied using fluorescent probes bound to actin subdomain 1 and the myosin head. Multistep changes in flexural rigidity of actin filament and in spatial arrangement of actin subdomain 1 and myosin SH1 helix in troponin-free ghost muscle fibers were revealed. During the ATPase cycle E117K tropomyosin inhibited the rotation of subdomain 1 by 46% and the tilt of the SH1 helix by 49% compared with wild-type. At strong-binding stages the proportion of strong binding sub-states in the actomyosin population is decreased by the mutation. At weak-binding stages abnormally high numbers of switched-on actin monomers were observed, thus indicating a disturbance in concerted conformational changes of actomyosin. These structural alterations are likely to underlie the contractile deficit observed with this mutation.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Karpicheva OE,Redwood CS,Borovikov YSdoi
10.1016/j.abb.2014.03.007subject
Has Abstractpub_date
2014-05-01 00:00:00pages
12-6eissn
0003-9861issn
1096-0384pii
S0003-9861(14)00096-4journal_volume
549pub_type
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