Actin-binding proteins such as alpha-actinin and severin share highly conserved structural domains across species from slime molds to vertebrates.
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Reveals deep evolutionary conservation of actin-binding domains; leaves open their roles in human cardiovascular cytoskeletal function.
DNA clones encoding the actin-binding proteins alpha-actinin and severin from Dictyostelium discoideum were isolated and sequenced. Comparisons of the deduced amino acid sequences with proteins from other species showed striking similarities at distinct regions. The F-actin cross-linking molecule alpha-actinin carries two characteristic EF-hand structures highly homologous to the Ca2+-binding loops of proteins from the calmodulin superfamily. An N-terminal region that is conserved in alpha-actinin from D. discoideum and vertebrates is also related to parts of the dystrophin sequence and might represent the F-actin binding site. Severin, gelsolin, villin, and fragmin share homologous sequences that are believed to participate in the severing activity of these proteins.
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Schleicher et al. (1988) studied this question.
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