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Construction and Analysis of Dictyostelium Mutants with Defects in Actin-Binding Proteins

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Part of the book series: Protoplasma ((PROTOPLASMA,volume 2))

Summary

Monoclonal antibodies against actin-binding proteins from the slime mould Dictyostelium discoideum were used to screen mutagenized cells in an attempt to select strains defective in specific components of the cytoskeleton. By a colony blot technique three mutants were detected that were defective in the F-actin crosslinking proteins aactinin and 120 kDa gelation factor and the F-actin fragmenting protein severin, respectively. Here we focus on the description of the a-actinin mutant HG 1130. Although this protein seems to be highly conserved throughout evolution, its loss did not impair the normal functions as e.g. motility, axenic growth, phagocytosis of bacteria, chemotaxis during development and formation of fruiting bodies. These surprising results suggest that evolutionary highly conserved proteins of the nonmuscle cytoskeleton may be replaced in their function by in vitro similarly acting proteins.

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Dedicated to Professor Dr. Noburo Kamiya on the occasion of his 75th birthday

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© 1988 Springer-Verlag

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Schleicher, M., Wallraff, E., Gerisch, G., Isenberg, G. (1988). Construction and Analysis of Dictyostelium Mutants with Defects in Actin-Binding Proteins. In: Tazawa, M. (eds) Cell Dynamics. Protoplasma, vol 2. Springer, Vienna. https://doi.org/10.1007/978-3-7091-9011-1_3

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  • DOI: https://doi.org/10.1007/978-3-7091-9011-1_3

  • Publisher Name: Springer, Vienna

  • Print ISBN: 978-3-7091-9013-5

  • Online ISBN: 978-3-7091-9011-1

  • eBook Packages: Springer Book Archive

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