Actin-binding proteins are conserved from slime molds to man.
Actin-binding proteins are conserved from slime molds to man.
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DOI：
10.1002/dvg.1020090428
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
M. Schleicher;E. André;H. Hartmann;A. Noegel
中科院分区：
文献类型：
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作者：
M. Schleicher;E. André;H. Hartmann;A. Noegel
分离并测序了盘状盘齿龙肌动蛋白结合蛋白α -肌动蛋白和severin的DNA克隆。将推导出的氨基酸序列与其他物种的蛋白质进行比较，在不同的区域显示出惊人的相似性。f -肌动蛋白交联分子α -肌动蛋白携带两个特征的EF-hand结构，与钙调蛋白超家族的Ca2+结合环高度同源。在盘状棘球鼠和脊椎动物的α -肌动蛋白中保守的n端区域也与部分肌营养不良蛋白序列有关，可能代表f -肌动蛋白结合位点。切断蛋白、凝胶蛋白、绒毛蛋白和片段蛋白共享同源序列，这些序列被认为参与这些蛋白的切断活性。
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.