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Genome-wide identification and characterization of myosin genes in the silkworm, Bombyx mori
Duan Tan1, Hai Hu1, Xiaoling Tong1
1State Key Laboratory of Silkworm Genome Biology, Key Laboratory of Sericultural Biology and Genetic Breeding, Ministry of Agriculture, College of Biotechnology, Southwest University, Chongqing 400715, China.
Abstract:
Myosins are a large family of actin filament-based motor proteins with a broad range of functions such as intracellular membrane trafficking, endocytosis, exocytosis, organellar transport, growth cone motility, cytokinesis, and cell locomotion. They are found in many organisms from fungi to humans. The myosin gene family in Bombyx mori is poorly studied, even though the molecular functions of these genes in vertebrates and insects, such as Drosophila, are well known. We identified 16 myosin genes from B. mori and identified the myosin genes in 12 vertebrates, eight insects, three nematodes, and seven protozoa. The number of myosin genes in vertebrates is double the number in invertebrates. The number of myosin isoforms in classes I and II is larger in vertebrates compared to invertebrates. B. mori myosin genes can be classified into 11 classes. Compared to B. mori, some myosin classes are not present in other insects. Classes I, II, XVIII, and XXI appear to be important for insect survival because they are conserved among nine insects. The relatively large sizes of B. mori myosin genes are due to their longer introns. Reverse transcription PCR (RT-PCR) and quantitative real-time PCR (qRT-PCR) analysis demonstrated that many B. mori myosin genes have tissue-specific expression and exhibit temporal-specific activity during metamorphosis. These data provide insights into evolutionary and functional aspects of B. mori myosin genes that could be useful for the study of homologous myosins in other Lepidoptera species.
Insights
This study identified 16 myosin genes in Bombyx mori, revealing evolutionary insights and tissue-specific expression patterns. These findings enhance understanding of myosin gene functions in insects and their evolutionary relationships.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Genomics
Background:
- Myosins are essential actin-based motor proteins involved in diverse cellular processes.
- While myosin functions are well-characterized in vertebrates and some insects, the myosin gene family in Bombyx mori remains understudied.
- Understanding myosin gene diversity and function is crucial for comprehending cellular mechanics and evolution.
Purpose of the Study:
- To identify and classify myosin genes in Bombyx mori.
- To compare the myosin gene repertoire of B. mori with other species across different taxa.
- To investigate the evolutionary conservation and expression patterns of B. mori myosin genes.
Main Methods:
- Bioinformatic identification of myosin genes in B. mori and comparative analysis with 12 vertebrates, 8 insects, 3 nematodes, and 7 protozoa.
- Phylogenetic classification of identified myosin genes into distinct classes.
- Reverse transcription PCR (RT-PCR) and quantitative real-time PCR (qRT-PCR) to analyze gene expression.
Main Results:
- Identified 16 myosin genes in B. mori, classified into 11 classes.
- Vertebrates possess double the number of myosin genes compared to invertebrates, with more isoforms in classes I and II.
- Classes I, II, XVIII, and XXI are conserved across nine insect species, suggesting importance for insect survival. B. mori myosin genes are larger due to longer introns.
- RT-PCR and qRT-PCR revealed tissue-specific expression and temporal activity during metamorphosis for many B. mori myosin genes.
Conclusions:
- The study provides a comprehensive catalog of myosin genes in B. mori, offering insights into their evolutionary history.
- Conserved myosin classes highlight key genes for insect survival and function.
- Tissue-specific and temporal expression patterns underscore the dynamic roles of myosins in B. mori development, particularly during metamorphosis.
- Findings facilitate comparative studies of homologous myosins in other Lepidoptera species.
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