Abstract:
:In this study, we investigated hybrid and non-hybrid actomyosin models including key contractile proteins: actin, myosin, and tropomyosin. These proteins were isolated from the rabbit skeletal muscle and the catch muscle of the mussel Crenomytilus grayanus. Our results confirmed literature data on an unusual ability of bivalve's tropomyosin to inhibit Mg-ATPase activity of skeletal muscle actomyosin. We have shown that the degree of inhibition depends on the environmental conditions and may vary within a wide range. The inhibitory effect of mussel tropomyosin was not detected in non-hybrid model (mussel myosin + mussel actin + mussel tropomyosin). This effect was revealed only in hybrid models containing mussel tropomyosin + rabbit (or mussel) actin + rabbit myosin. We assume that mussel and rabbit myosins have mismatched binding sites for actin. In addition, mussel tropomyosin interacting with actin is able to close the binding sites of rabbit myosin with actin, which leads to inhibition of Mg-ATPase activity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Shelud'ko NS,Vyatchin IG,Lazarev SS,Shevchenko UVdoi
10.1016/j.bbrc.2015.07.023subject
Has Abstractpub_date
2015-08-21 00:00:00pages
611-5issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(15)30254-0journal_volume
464pub_type
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