ArticleThe Journal of biological chemistry2014
A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- Molecular features of myosin F adapted for driving actin flows in Toxoplasma gondii.Journal of cell science · 2026Article
- Molecular features of Myosin F adapted for driving actin flows inbioRxiv : the preprint server for biology · 2025Article
- Expression, Purification, and In Vitro Analysis of Myosin.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance in Toxoplasma gondii.PLoS pathogens · 2024Article
- Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance inbioRxiv : the preprint server for biology · 2024Article
- New advances in immune mechanism and treatment during ocular toxoplasmosis.Frontiers in immunology · 2024Review
- MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii.PLoS biology · 2023Article
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- Structural role of essential light chains in the apicomplexan glideosome.Communications biology · 2020Article
- The Myosin Family of Mechanoenzymes: From Mechanisms to Therapeutic Approaches.Annual review of biochemistry · 2020Review
- Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Calcium signaling and the lytic cycle of the Apicomplexan parasite Toxoplasma gondii.Biochimica et biophysica acta. Molecular cell research · 2018Review
- Reconstitution of the core of the malaria parasite glideosome with recombinantThe Journal of biological chemistry · 2017Article
- Dissecting the molecular assembly of theThe Journal of biological chemistry · 2017Article
- Gliding motility powers invasion and egress in Apicomplexa.Nature reviews. Microbiology · 2017Review
- Compositional and expression analyses of the glideosome during theThe Journal of biological chemistry · 2017Article
- Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Molecular Basis of Erythrocyte Invasion by Malaria Parasites.Cell host & microbe · 2017Review
- Myosin-dependent cell-cell communication controls synchronicity of division in acute and chronic stages of Toxoplasma gondii.Nature communications · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Many diverse myosin classes can be expressed using the baculovirus/Sf9 insect cell expression system, whereas others have been recalcitrant. We hypothesized that most myosins utilize Sf9 cell chaperones, but others require an organism-specific co-chaperone. TgMyoA, a class XIVa myosin from the parasite Toxoplasma gondii, is required for the parasite to efficiently move and invade host cells. The T. gondii genome contains one UCS family myosin co-chaperone (TgUNC). TgMyoA expressed in Sf9 cells was soluble and functional only if the heavy and light chain(s) were co-expressed with TgUNC. The tetratricopeptide repeat domain of TgUNC was not essential to obtain functional myosin, implying that there are other mechanisms to recruit Hsp90. Purified TgMyoA heavy chain complexed with its regulatory light chain (TgMLC1) moved actin in a motility assay at a speed of ∼1.5 μm/s. When a putative essential light chain (TgELC1) was also bound, TgMyoA moved actin at more than twice that speed (∼3.4 μm/s). This result implies that two light chains bind to and stabilize the lever arm, the domain that amplifies small motions at the active site into the larger motions that propel actin at fast speeds. Our results show that the TgMyoA domain structure is more similar to other myosins than previously appreciated and provide a molecular explanation for how it moves actin at fast speeds. The ability to express milligram quantities of a class XIV myosin in a heterologous system paves the way for detailed structure-function analysis of TgMyoA and identification of small molecule inhibitors.
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Registered trials
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.