Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Native bare zone assemblage nucleates myosin filament assembly

R Niederman, L K Peters

    Journal of Molecular Biology
    |November 15, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Pandemic Considerations on Essential Oral Health Care.

    Journal of dental research·2020
    Same author

    Nuclear F-actin Cytology in Oral Epithelial Dysplasia and Oral Squamous Cell Carcinoma.

    Journal of dental research·2020
    Same author

    Quality Appraisal of Child Oral Health-Related Quality of Life Measures: A Scoping Review.

    JDR clinical and translational research·2019
    Same author

    An Economic Evaluation of a Comprehensive School-Based Caries Prevention Program.

    JDR clinical and translational research·2019
    Same author

    Economic Evaluations of School Sealant Programs and the Consent Conundrum.

    Journal of dental research·2018
    Same author

    School-Based Caries Prevention, Tooth Decay, and the Community Environment.

    JDR clinical and translational research·2018
    Same journal

    UPF3A and UPF3B shape the transcriptome cooperatively yet oppose cell function.

    Journal of molecular biology·2026
    Same journal

    Antibody-secreting cells integrate efficient NMD with non‑canonical UPR signaling to maintain proteostasis and support massive immunoglobulin synthesis.

    Journal of molecular biology·2026
    Same journal

    Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

    Journal of molecular biology·2026
    Same journal

    UPF1 at Work: Structural and Mechanistic Insights Into a Master Regulator of Nonsense-Mediated mRNA Decay.

    Journal of molecular biology·2026
    Same journal

    Structural basis for the pro-amyloidogenic action and ligand binding of a novel W72R variant of human apolipoprotein A-I.

    Journal of molecular biology·2026
    Same journal

    Cryo-EM Structure of the C. Elegans Septin Tetramer Reveals a Revised Architecture and Conserved Positional Orthology.

    Journal of molecular biology·2026
    See all related articles

    The myosin bare zone assemblage nucleates myosin filament assembly. Isolated bare zone components retain their length, while distal myosin molecules reassemble into longer filaments, refining models of myosin filament formation.

    Area of Science:

    • Muscle biology
    • Biochemistry
    • Protein assembly

    Background:

    • Myosin filaments are essential for muscle contraction.
    • Their assembly is thought to involve antiparallel and parallel aggregation of myosin subunits.
    • Filament length control mechanisms, such as self-assembly or Vernier processes, are debated.

    Purpose of the Study:

    • To investigate the role of the myosin bare zone assemblage in nucleating myosin filament assembly.
    • To refine current models of myosin filament length regulation.

    Main Methods:

    • Dialysis of native myosin filaments to alter ionic conditions (pH 8 or 0.2 M-KCl).
    • Separation of bare zone assemblages and distal myosin molecules via column chromatography.
    • Reassembly experiments using isolated components and mixtures.

    Related Experiment Videos

    Main Results:

    • Native myosin filaments are typically 1.5 micrometers long.
    • Dialysis to pH 8 or 0.2 M-KCl yields a ~0.3 micrometer bare zone assemblage.
    • Reassembly in 0.1 M-KCl reforms 1.5 micrometer filaments.
    • Fractionated bare zone assemblages remain ~0.3 micrometer, while distal molecules form ~5 micrometer filaments.
    • Mixed components form filaments whose length depends on the amount of distal myosin.

    Conclusions:

    • The intact myosin bare zone assemblage acts as a nucleation site for myosin filament assembly.
    • Myosin filament length is regulated by the interplay between the bare zone and distal myosin molecules.
    • The bare zone's nucleating capacity may involve bare zone myosin or M band components.