Actin-binding proteins are conserved from slime molds to man.
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.
Schleicher
M
M
Max-Planck-Institute for Biochemistry, Martinsried, Federal Republic of Germany.
André
E
E
Hartmann
H
H
Noegel
A A
AA
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002352:Carrier Proteins / Q000235:genetics*; D004271:DNA, Fungal / Q000235:genetics / Q000302:isolation & purification; D004023:Dictyostelium / Q000235:genetics*; D005656:Fungal Proteins / Q000235:genetics*; D005796:Genes; D005800:Genes, Fungal; D006801:Humans; D008840:Microfilament Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D002352:Carrier Proteins; D004271:DNA, Fungal; C034037:F-actin-binding proteins; D005656:Fungal Proteins; D008840:Microfilament Proteins