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Updated: Sep 29, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Proteolytic substructure of myorod, a thick filament protein of molluscan smooth muscles
N Shelud'ko1, K Tuturova, T Permyakova
1Department of Cell Biophysics, Institute of Marine Biology, Far East Division of Russian Academy of Sciences, Vladivostok 690041, Russia. sheludko@stl.ru
Abstract:
Myorod (MR), a new thick filament protein of molluscan smooth muscles, is an alternatively spliced product of the myosin (Mn) heavy chain gene. We studied digestion of MR and Mn from the posterior adductor of Crenomytilus grayanus and the outer portion of adductor of Mizuchopecten (Patinopecten) yessoensis by papain and constructed the proteolytic substructure of MR, that is an analogue to Mn substructure. There are a head domain (analogue of Mn S1) and a rod domain (analogue of Mn rod); the junction between them is split at low ionic strength. The rod, in turn, consists of a neck domain (analogue of Mn S2) and a tail domain (identical to light meromyosin); the junction between them is split at high ionic strength. The localization and possible function of MR are discussed.
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