Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility.
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Summary
Examination of the effects of crosslinking of monomeric and polymeric actin with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, disuccinimidyl suberate and glutaraldehyde on the interaction with heavy meromyosin in solution and on the sliding movement concluded that movement is generated by interaction of myosin with segments of F-actin containing a number of intact monomers.
- Type
- article
- Published
- 1990-12-05
- Cited by
- 91
- References
- 34
- OpenAlex
- https://openalex.org/W2091442492
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:21434879
Keywords
Glutaraldehyde, Actin, Heavy meromyosin, Myosin, Biophysics
References
- The ATPase mechanism of skeletal and smooth muscle acto-subfragment 1.
- Monomeric Acanthamoeba myosins I support movement in vitro.
- Chicken-gizzard actin. Interaction with skeletal-muscle myosin.
- Effects of specific chemical modification of actin.
- Activation of H-meromyosin ATPase by polymers of actin and carboxymethylated actin.
- Control of muscle contraction
- Studies on spin-labeled actin.
- Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle
- Electronmicroscopic investigation of the flexibility of F-actin.
- Calcium-sensitive binding of heavy meromyosin to regulated actin requires light chain 2 and the head-tail junction.
- Functional characterization of skeletal F-actin labeled on the NH2-terminal segment of residues 1-28.
- Direct observation of motion of single F-actin filaments in the presence of myosin
- An improved assay for nanomole amounts of inorganic phosphate.
- Structure of the actin–myosin interface
- Investigation, by cross-linking, of conformational changes in F-actin during its interactions with myosin.
- Mechanism of adenosine triphosphate hydrolysis by actomyosin.
- Sliding movement of single actin filaments on one-headed myosin filaments
- Reaction of proteins with glutaraldehyde.
- Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay.
- Pulse-fluorometry study on actin and heavy meromyosin using F-actin labelled with N-(1-pyrene)maleimide.
Cited by
- Myosin light chain kinase from skeletal muscle regulates an ATP-dependent interaction between actin and myosin by binding to actin
- Dethiophalloidin increases Ca2+ responsiveness of skinned cardiac muscle
- Muscle contraction mechanism based on actin filament rotation.
- Effect of intramolecular cross-linking between glutamine-41 and lysine-50 on actin structure and function
- Actin allostery again?
- Intermonomer flexibility of Ca- and Mg-actin filaments at different pH values.
- Actin Age Orchestrates Myosin-5 and Myosin-6 Runlengths
- The Role of Structural Dynamics of Actin in Class-Specific Myosin Motility
- Antibodies Covalently Immobilized on Actin Filaments for Fast Myosin Driven Analyte Transport
- Dominant Negative Mutant Actins Identified in Flightless Drosophila Can Be Classified into Three Classes*
- Inter-monomer cross-linking affects the thermal transitions in F-actin
- Myosin filament ATPase is enhanced by intramolecularly cross-linked actin
- Structural implications of the chemical modification of Cys(10) on actin.
- Orientation and Mobility of Actin in Different Intermediate States of the ATP Hydrolysis Cycle
- Microsecond rotational dynamics of F-actin in ActoS1 filaments during ATP hydrolysis.
- Dynamic polymorphism of actin as activation mechanism for cell motility
- Thermal fluctuations biased for directional motion in molecular motors
- Caged protein conjugates and light-directed generation of protein activity: preparation, photoactivation, and spectroscopic characterization of caged G-actin conjugates.
- Probing the structure of F-actin: cross-links constrain atomic models and modify actin dynamics.
- Remodeling of actin filaments by ADF/cofilin proteins
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