ArticleThe Journal of cell biology1982
A novel 36,000-dalton actin-binding protein purified from microfilaments in Physarum plasmodia which aggregates actin filaments and blocks actin-myosin interaction.
Article in The Journal of cell biology, 1982. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Mechanisms of cell shape change: the cytomechanics of cellular response to chemical environment and mechanical loading.The Journal of cell biology · 1992Article
- Dynamic aspects of the contractile system in Physarum plasmodium. III. Cyclic contraction-relaxation of the plasmodial fragment in accordance with the generation-degeneration of cytoplasmic actomyosin fibrils.The Journal of cell biology · 1987Article
- Rheological properties of living cytoplasm: endoplasm of Physarum plasmodium.The Journal of cell biology · 1983Article
- A 72,000-mol-wt protein from tomato inhibits rabbit acto-S-1 ATPase activity.The Journal of cell biology · 1983Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the plasmodia of Physarum polycephalum, which show a cyclic contraction-relaxation rhythm of the gel layer, huge aggregates of entangled actin microfilaments are formed at about the onset of the relaxation (R. Nagai, Y. Yoshimoto, and N. Kamiya. 1978. J. Cell Sci. 33:205-225). By treating the plasmodia with Triton X-100, we prepared a demembranated cytoskeleton consisting of entangled actin filaments and found that the actin filaments hardly interact with rabbit skeletal myosin. From the cytoskeleton we purified a novel actin-binding protein which binds stoichiometrically to actin and makes actin filaments curled and aggregated. It also inhibits the ATPase activity as well as the superprecipitation of reconstituted rabbit skeletal muscle actomyosin. This protein has a polypeptide molecular weight of 36,000 and binds 7 mol of actin/mol 36,000 polypeptide.
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