Abstract
As the main structural protein of muscle fiber, myosin is essential for multiple cellular processes or functions, especially for muscle composition and development. Although the shrimp possess a well-developed muscular system, the knowledge about the myosin family in shrimp is far from understood. In this study, we performed comprehensive analysis on the myosin genes in the genome of the Pacific white shrimp, Litopenaeus vannamei. A total of 29 myosin genes were identified, which were classified into 14 subfamilies. Among them, Myo2 subfamily was significantly expanded in the penaeid shrimp genome. Most of the Myo2 subfamily genes were primarily expressed in abdominal muscle, which suggested that Myo2 subfamily genes might be responsible for the well-developed muscular system of the penaeid shrimp. In situ hybridization detection showed that the slow-type muscle myosin gene was mainly localized in pleopod muscle and superficial ventral muscle of the shrimp. This study provides valuable insights into the evolutionary and functional characterization of myosin genes in shrimps, which provides clues for us to understand the well-developed muscular system of shrimp.
Highlights
Most eukaryotic cells possess myosin proteins, which bind to filamentous actin and produce physical forces through ATP hydrolysis (Richards and Cavalier-Smith, 2005; Sebé-Pedrós et al, 2014)
A total of 29 myosin genes were identified in L. vannamei, including 15 muscle-type Myo2 genes, one non-muscle type Myo2 gene and 13 unconventional myosin genes (Table 1)
The gene structure of these 29 myosin genes showed high complexity with the sizes ranging from 6.159 to 171.807 kb that corresponded to encode proteins of 1,010-2,158 aa (Table 1)
Summary
Most eukaryotic cells possess myosin proteins, which bind to filamentous actin and produce physical forces through ATP hydrolysis (Richards and Cavalier-Smith, 2005; Sebé-Pedrós et al, 2014). The Myo subfamily (Myosin 2), known as myosin heavy chain (MYH or MHC), are the main component of the contractile muscle. They are considered to be conventional myosins, while the other subfamilies are considered to be unconventional myosins. The Myo subfamily genes can be classified into three groups, including fasttype, slow-type and non-muscle type. The Myo subfamily proteins can form large bipolar filaments through tail-directed homo-oligomerization, while the tails of the unconventional myosins typically direct binding to membrane and other proteins (Woolner and Bement, 2009)
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