Schleicher M, André E, Hartmann H, Noegel A A
Max-Planck-Institute for Biochemistry, Martinsried, Federal Republic of Germany.
Dev Genet. 1988;9(4-5):521-30. doi: 10.1002/dvg.1020090428.
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.
分离并测序了编码盘基网柄菌肌动蛋白结合蛋白α-辅肌动蛋白和肌割蛋白的DNA克隆。将推导的氨基酸序列与其他物种的蛋白质进行比较，发现在不同区域存在显著相似性。F-肌动蛋白交联分子α-辅肌动蛋白带有两个与钙调蛋白超家族蛋白质的Ca2+结合环高度同源的特征性EF手结构。盘基网柄菌和脊椎动物的α-辅肌动蛋白中保守的N端区域也与肌营养不良蛋白序列的部分相关，可能代表F-肌动蛋白结合位点。肌割蛋白、凝溶胶蛋白、绒毛蛋白和片段蛋白共享同源序列，据信这些序列参与了这些蛋白质的切断活性。
