ArticleProceedings of the National Academy of Sciences of the United States of America1993
Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 90 citations in OpenAlex.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.Life science alliance · 2023Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- Article
- Metal cation controls phosphate release in the myosin ATPase.Protein science : a publication of the Protein Society · 2017Article
- The Conserved Lysine-265 Allosterically Modulates Nucleotide- and Actin-binding Site Coupling in Myosin-2.Scientific reports · 2017Article
- Comparison of elementary steps of the cross-bridge cycle in rat papillary muscle fibers expressing α- and β-myosin heavy chain with sinusoidal analysis.Journal of muscle research and cell motility · 2016Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- Macromolecular Crowding Modulates Actomyosin Kinetics.Biophysical journal · 2016Article
- High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinetic characterization of the sole nonmuscle myosin-2 from the model organism Drosophila melanogaster.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Metal cation controls myosin and actomyosin kinetics.Protein science : a publication of the Protein Society · 2013Article
- Metal switch-controlled myosin II from Dictyostelium discoideum supports closure of nucleotide pocket during ATP binding coupled to detachment from actin filaments.The Journal of biological chemistry · 2013Article
- Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2.The Journal of biological chemistry · 2013Article
- Erratum to: Identification of functional differences between recombinant human α and β cardiac myosin motors.Cellular and molecular life sciences : CMLS · 2012Article
- Mn(2+)-nucleotide coordination at the myosin active site as detected by pulsed electron paramagnetic resonance.The journal of physical chemistry. B · 2012Article
- Allosteric communication in Dictyostelium myosin II.Journal of muscle research and cell motility · 2012Article
- G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility.The Journal of biological chemistry · 2012Article
- Identification of functional differences between recombinant human α and β cardiac myosin motors.Cellular and molecular life sciences : CMLS · 2012Article
- Functional characterization of the human myosin-7a motor domain.Cellular and molecular life sciences : CMLS · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A detailed kinetic study of the interaction of a recombinant myosin head fragment (MHF) of Dictyostelium discoideum with actin and adenine nucleotides has been made by using a combination of rapid-reaction, equilibrium, and fluorescence methods. MHF is equivalent in size to a proteolytic fragment of skeletal muscle myosin, subfragment 1 (S1), the simplest unit of myosin to retain enzymatic and functional activity. The results show that qualitatively the interactions of MHF with nucleotides and actin are the same as those of S1. Both bind to rabbit actin with the same affinity, although differences in the rate constants of their interactions with nucleotides in the presence and absence of actin occur. The rate of ATP binding to MHF and the subsequent cleavage step are significantly slower than the corresponding rates with S1. The dissociation of a fluorescent analog of ADP from MHF was 5-fold faster than from S1, while its rate of binding MHF was 3-fold slower, resulting in a weaker association equilibrium constant. The ATP-induced isomerization of the actoMHF complex was 10-fold slower than for actoS1, but the binding affinities of ADP for actoMHF and actoS1 were indistinguishable. The results suggest a different degree of coupling between the nucleotide and actin binding sites of MHF and S1 which may be a common feature of nonmuscle myosins. They also provide the basis for a study of specifically modified myosins with which one can probe the sites of interaction with nucleotides or actin, as well as functional motility.
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