Further purification and characterization of slime mold myosin and slime mold actin

Adelman, Mark R.; Taylor, E. W.

doi:10.1021/bi00840a047

Cited by 134 publications

(45 citation statements)

References 47 publications

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“…Protozoa In addition to the structural characteristics used here, actin should also be identified by biochemical criteria, including molecular weight, amino-acid analysis, and activation of myosin ATPase (24)(25)(26). Preliminary evidence indicates the presence of a band with the same mobility as actin on gels loaded with material from an extract of an acetone powder prepared from Nitella.…”

Section: Discussionmentioning

confidence: 99%

Actin in the Green Alga, Nitella

Palevitz

Ash

Hepler

1974

Proc. Natl. Acad. Sci. U.S.A.

158

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Bundles of microfilaments very similar in appearance to actin are present in cytoplasmic suspensions obtained from Nitella flexilis. The microfilaments bind rabbit heavy meromyosin in arrowhead arrays similar to those produced on muscle actin. The arrowheads are removed with ATP. The results provide evidence that actin is present in green plants, probably in the form of microfilaments thought to be involved in cytoplasmic streaming.

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Section: Discussionmentioning

confidence: 99%

Actin in the Green Alga, Nitella

Palevitz

Ash

Hepler

1974

Proc. Natl. Acad. Sci. U.S.A.

158

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“…, including blood platelets (2,3), leucocytes (4), mammalian brain (5), sarcoma cells (6), seaurchin eggs (7), Acanthamoeba castellanii (8), plasmodia of the acellular slime mold, Physarum polycephalum (9)(10)(11), amoebae of the cellular slime mold, Dictyostelium discoideum (12), and most recently in epithelial cells of the chicken intestine (13). The similarity of these actin-like proteins with muscle actin is emphasized by the observations (11)(12)(13)(14)(15)(16)) that they interact with muscle heavy meromyosin (HMM) to give "arrowheads" similar to those originally observed by Huxley with muscle acto-HMM (17).…”

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confidence: 99%

Cytochalasin B, Its Interaction with Actin and Actomyosin from Muscle

Spudich

Lin

1972

Proc. Natl. Acad. Sci. U.S.A.

140

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Cytochalasin B, an alkaloid that inhibits a wide variety of cellular movements, interacts with actomyosin, the contractile protein complex of striated muscle. This interaction causes a decrease in viscosity of the actomyosin complex and an inhibition of acto-heavy meromyosin ATPase activity of at least 60%. Cytochalasin B does not affect the viscosity of myosin nor the ATPase activity of heavy meromyosin, suggesting that the drug might interact directly with the actin moiety of the actomyosin complex. Indeed, as judged by viscometry, there is a strong interaction of cytochalasin B with actin, at nearly stoichiometric concentrations. Myosin appears to compete with cytochalasin for binding to actin. (1), including blood platelets (2, 3), leucocytes (4), mammalian brain (5), sarcoma cells (6), seaurchin eggs (7), Acanthamoeba castellanii (8), plasmodia of the acellular slime mold, Physarum polycephalum (9-11), amoebae of the cellular slime mold, Dictyostelium discoideum (12), and most recently in epithelial cells of the chicken intestine (13). The similarity of these actin-like proteins with muscle actin is emphasized by the observations (11-16) that they interact with muscle heavy meromyosin (HMM) to give "arrowheads" similar to those originally observed by Huxley with muscle acto-HMM (17).Another indication that the molecular basis of many forms of movement may be related comes from studies using the drug cytochalasin B. This alkaloid, a metabolite of the fungus Helminthosporium dematioideum (18), inhibits a wide variety of cellular movements (18)(19)(20). To our knowledge, nothing is known about the mode of action of cytochalasin B at the molecular level.Since actomyosin-like proteins and cytochalasin B have both been implicated in cellular movement in several orgaAbbreviations: Actin, filamentous actin or F-actin (the monomer is specified as G-actin); CB-actin, actin saturated with cytochalasin B; Me2SO, dimethyl sulfoxide; HMM, heavy meromyosin (a proteolytic fragment of myosin retaining ATPase activity and the ability to interact with actin). 442 nisms, we have begun to investigate whether cytochalasin B inhibits movement by interacting with actomyosin-like proteins. We report here that cytochalasin B interacts with purified muscle actin and that it appears to compete with myosin for binding to the actin. experiments. In the first, the actomyosin complex was formed before the addition of cytochalasin; in thie second, the actomyosin complex was formed after the addition of cytochalasin.The results of the first experiment were as follows (Fig. 1, open circles). Addition of actin to myosin in a 5:1 molar ratio caused an increase in the viscosity of the solution to a value

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“…13) resembles the heavy meromyosin crosslinks of striated muscle (22) . There is extensive evidence in the literature which suggests that microfilaments from a wide variety of nonmuscle cells are actin-like due to their binding of heavy meromyosin (23)(24)(25) and their chemical properties (26) . There is also evidence that myosin-like proteins are present in such nonmuscle cells (e .g., 26) .…”

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The Effects of Cytochalasin B on the Microfilaments of Baby Hamster Kidney (Bhk-21) Cells

Goldman

1972

The Journal of Cell Biology

107

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Attempts were made to test the motile functions of bundles of microfilaments found in baby hamster kidney (BHK-21) cells, by using cytochalasin B (CB) . It was found that individual cells respond differently to the drug . These differential effects are quite obvious in both light and electron microscope preparations . Some cells contain normal bundles of microfilaments even after 24 hr in CB, and other cells form muscle-like configurations which also contain arrays of microfilaments . These varied effects suggest the existence of several types of microfilaments in BHK-21 cells, and make the interpretation of the motif role of microfilaments difficult to evaluate at the present time .

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Further purification and characterization of slime mold myosin and slime mold actin

Cited by 134 publications

References 47 publications

Actin in the Green Alga, Nitella

Actin in the Green Alga, Nitella

Cytochalasin B, Its Interaction with Actin and Actomyosin from Muscle

The Effects of Cytochalasin B on the Microfilaments of Baby Hamster Kidney (Bhk-21) Cells

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