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Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
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Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
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A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
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Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
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Myosin II sequences for Lethocerus indicus.

Lanette Fee1, Weili Lin2, Feng Qiu2

  • 1Department of Cell Biology, Duke University, Box 3011, Durham, NC, 27705, USA.

Journal of Muscle Research and Cell Motility
|July 15, 2017
PubMed
Summary
This summary is machine-generated.

Researchers sequenced myosin II genes from the giant waterbug, Lethocerus indicus. Alternative splicing in these ancient genes may influence the unique structure of their thick filaments.

Keywords:
Alternative splicingInsect flight muscleInteracting heads motifMyosin II

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Area of Science:

  • Molecular Biology
  • Genomics
  • Structural Biology

Background:

  • Myosin II is a motor protein essential for muscle contraction and other cellular processes.
  • The structure of myosin filaments varies across different species, influencing their function.
  • The giant waterbug (Lethocerus indicus) possesses a unique thick filament structure.

Purpose of the Study:

  • To characterize the genomic and expressed myosin II sequences of Lethocerus indicus.
  • To investigate the role of alternative splicing in the structure and stability of myosin filaments.
  • To understand the structural basis for the perpendicular interacting heads motif in Lethocerus myosin.

Main Methods:

  • Genomic DNA and complementary DNA (cDNA) sequencing.
  • Bioinformatic analysis of myosin II gene structure and alternative splicing.
  • Comparative analysis of myosin II sequences and filament structures across species.

Main Results:

  • The Lethocerus indicus myosin II gene is intron-rich and appears ancient.
  • Six regions of mutually exclusive exons undergo alternative splicing.
  • The myosin S2 domain lacks negative charge, correlating with a perpendicular interacting heads motif.

Conclusions:

  • Alternative splicing in Lethocerus myosin II likely contributes to the asymmetric dimer structure and filament stabilization.
  • The unique S2 domain charge explains the perpendicular interacting heads motif, differentiating it from other species.
  • This study provides insights into myosin evolution and the structural diversity of muscle filaments.