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

Interaction between actin and HMM.

J Borejdo, M Giordano

    Biochemical and Biophysical Research Communications
    |December 15, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Actin and heavy meromyosin (HMM) interact to form a gel with MgATP, demonstrating muscle contraction can occur without myosin filaments. Soluble myosin heads effectively drive mechanical effects by binding to actin.

    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

    Photophysical properties of 2-Phenylindole in poly (vinyl alcohol) film at room temperature. Enhanced phosphorescence anisotropy with direct triplet state excitation.

    Methods and applications in fluorescence·2019
    Same author

    Mesoscopic analysis of motion and conformation of cross-bridges.

    Biophysical reviews·2017
    Same author

    Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.

    American journal of physiology. Heart and circulatory physiology·2015
    Same author

    The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse hearts.

    Biochemistry·2014
    Same author

    Cross-bridge kinetics in myofibrils containing familial hypertrophic cardiomyopathy R58Q mutation in the regulatory light chain of myosin.

    Journal of theoretical biology·2011
    Same author

    Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.

    Journal of molecular and cellular cardiology·2011
    Same journal

    Quercetin suppresses TGF-β1-induced proliferation and migration of vascular smooth muscle cells via the Smad2/3/MMP-9 signaling axis.

    Biochemical and biophysical research communications·2026
    Same journal

    Biosynthesis, characterization and biological potential of microbe-mediated silver nanoparticles using thermophilic actinomycetes, Streptomyces nigra.

    Biochemical and biophysical research communications·2026
    Same journal

    COP9 signalosome 8 mediated autophagy drives proliferation, invasion, and metastasis in pancreatic ductal adenocarcinoma.

    Biochemical and biophysical research communications·2026
    Same journal

    Tumor budding in colorectal cancer: partial EMT, microenvironmental remodeling, and metastatic competence.

    Biochemical and biophysical research communications·2026
    Same journal

    Exploring the therapeutic versatility and multitarget pharmacological potential of acyl hydrazone-hydrazide scaffolds.

    Biochemical and biophysical research communications·2026
    Same journal

    The plasma membrane H<sup>+</sup>-ATPase OSA2 negatively regulates salt tolerance in rice seedlings.

    Biochemical and biophysical research communications·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Muscle Physiology

    Background:

    • Muscle contraction involves actin and myosin interactions.
    • Heavy meromyosin (HMM) is a proteolytic fragment of myosin.
    • Myosin filament formation is traditionally considered essential for muscle contraction.

    Purpose of the Study:

    • To investigate the mechanochemical interaction between actin and HMM in the absence of intact myosin filaments.
    • To determine if soluble myosin heads are sufficient for generating mechanical effects.
    • To provide evidence for the ability of individual HMM heads to bind distinct actin filaments.

    Main Methods:

    • Biochemical assays to observe the interaction between purified actin and HMM.
    • Addition of MgATP to induce gel formation.

    Related Experiment Videos

  • Microscopic or biophysical techniques to analyze binding interactions (implied).

    • Main Results:

    • Actin and HMM rapidly form a precipitate (gel) upon MgATP addition.
    • This reaction demonstrates that myosin filament formation is not a prerequisite for mechanochemical activity.
    • Evidence supports that each head of an HMM molecule can bind to a separate actin filament.

    Conclusions:

    • Soluble myosin heads are competent to interact with actin and produce mechanical effects, such as contraction.
    • Myosin filament assembly is not essential for the fundamental mechanochemical processes in muscle.
    • The study supports a model where HMM heads can engage with multiple actin filaments simultaneously.