ArticleBiophysical journal1999
Cooperativity between two heads of dictyostelium myosin II in in vitro motility and ATP hydrolysis.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Molecular characterization and subcellular localization of Arabidopsis class VIII myosin, ATM1.The Journal of biological chemistry · 2014Article
- Gene transfer, expression, and sarcomeric incorporation of a headless myosin molecule in cardiac myocytes: evidence for a reserve in myofilament motor function.American journal of physiology. Heart and circulatory physiology · 2011Article
- Expression of Y53A-actin in Dictyostelium disrupts the cytoskeleton and inhibits intracellular and intercellular chemotactic signaling.The Journal of biological chemistry · 2010Article
- Mutation of actin Tyr-53 alters the conformations of the DNase I-binding loop and the nucleotide-binding cleft.The Journal of biological chemistry · 2010Article
- Tropomyosin dynamics in cardiac thin filaments: a multisite forster resonance energy transfer and anisotropy study.Biophysical journal · 2008Article
- Dictyostelium myosin II mechanochemistry promotes active behavior of the cortex on long time scales.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- A mutant heterodimeric myosin with one inactive head generates maximal displacement.The Journal of cell biology · 2003Article
- Coevolution of head, neck, and tail domains of myosin heavy chains.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
To elucidate the significance of the two-headed structure of myosin II, we have engineered and characterized recombinant single-headed myosin II. A tail segment of a myosin II heavy chain fused with a His-tag was expressed in wild-type Dictyostelium cells. Single-headed myosin, which consists of a full length myosin heavy chain and a tagged tail, was isolated on the basis of the affinities for Nickel agarose and actin. Actin sliding velocity by the single-headed myosin was about half of the two-headed, whereas the minimum density of the heads to support continuous movement was twofold higher. Actin-activated MgATPase activity of the single-headed myosin in solution in the presence of 24 microM actin was less than half of the two headed. This decrease is primarily because of fourfold-elevated Kapp for actin and secondary to 40% lower Vmax. These results suggest that the two heads of a Dictyostelium myosin II molecule act cooperatively on an actin filament. We propose a mechanism by which two heads move actin efficiently based on the cooperativity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.