Abstract
Myosins are important eukaryotic motor proteins that bind actin and utilize the energy of ATP hydrolysis to perform a broad range of functions such as muscle contraction, cell migration, cytokinesis, and intracellular trafficking. However, the characterization and function of myosin is poorly studied in teleost fish. In this study, we identified 60 myosin family genes in a marine teleost, black rockfish (Sebastes schlegelii), and further characterized their expression patterns. myosin showed divergent expression patterns in adult tissues, indicating they are involved in different types and compositions of muscle fibers. Among 12 subfamilies, S. schlegelii myo2 subfamily was significantly expanded, which was driven by tandem duplication events. The up-regulation of five representative genes of myo2 in the skeletal muscle during fast-growth stages of juvenile and adult S. schlegelii revealed their active role in skeletal muscle fiber synthesis. Moreover, the expression regulation of myosin during the process of myoblast differentiation in vitro suggested that they contribute to skeletal muscle growth by involvement of both myoblast proliferation and differentiation. Taken together, our work characterized myosin genes systemically and demonstrated their diverse functions in a marine teleost species. This lays foundation for the further studies of muscle growth regulation and molecular mechanisms of indeterminate skeletal muscle growth of large teleost fishes.
Highlights
Myosins are a large family of cytoskeletal motor proteins that bind filamentous actin and utilize the energy of ATP hydrolysis to play an important part in divergent biological process, such as muscle contraction, cell motility and contractility, cytokinesis, and intracellular trafficking [1,2,3]
In S. schlegelii, we identified and characterized 60 myosin genes, containing 27 conventional myosin genes, which belong to Myo2 subfamily
We identified and characterized 60 myosin family genes in S. schlegelii and demonstrated the expansion of myo2 subfamily in this species
Summary
Myosins are a large family of cytoskeletal motor proteins that bind filamentous actin and utilize the energy of ATP hydrolysis to play an important part in divergent biological process, such as muscle contraction, cell motility and contractility, cytokinesis, and intracellular trafficking [1,2,3]. Myosins are typically composed of three domains, a conserved head located in the N-terminal that binds to actin filaments, a short neck as a binding site for myosin light chain, and a tail located in the C-terminal generally binding to the motor “cargo” to determine the functions of the motor [7,8]. Eukaryotes contain up to 35 myosin subfamilies based on an analysis of 2269 Myosin motor domains from 328 organisms [9]. The myo subfamily, as known as myosin 2 (myosin heavy chain, MYH or MHC), is considered to be the conventional myosin, which is the main component of skeletal muscle whereas the other myosin subfamilies are considered to be unconventional myosin [10]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
