Yonezawa N, Nishida E, Iida K, Kumagai H, Yahara I, Sakai H
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
J Biol Chem. 1991 Jun 5;266(16):10485-9.
Cofilin is an F-actin side-binding and -depolymerizing protein with an apparent molecular mass of 21 kDa. By means of the end label fingerprinting method, the amino acid residue on cofilin sequence cross-linked to actin by zero length cross-linker, 1-ethyl-3-(3-dimethylamino propyl)carbodiimide, was identified as Lys112 and/or Lys114. A synthetic dodecapeptide patterned on the sequence around the actin-cross-linking site of cofilin (Trp104-Met115) inhibited the binding of cofilin to actin. Moreover, the dodecapeptide was found to be a potent inhibitor of actin polymerization. Thus, we conclude that the dodecapeptide sequence constitutes the region essential for the actin-binding and -depolymerizing activity of cofilin. A sequence similar to the dodecapeptide is found in other actin-depolymerizing proteins, destrin, actin-depolymerizing factor, and depactin. Therefore, the dodecapeptide sequence may be a consensus sequence essential for actin-binding and -depolymerizing activity in actin-depolymerizing proteins.
丝切蛋白是一种F-肌动蛋白侧链结合和解聚蛋白，表观分子量为21 kDa。通过末端标记指纹法，确定了丝切蛋白序列上通过零长度交联剂1-乙基-3-(3-二甲基氨基丙基)碳二亚胺与肌动蛋白交联的氨基酸残基为Lys112和/或Lys114。一种基于丝切蛋白（Trp104-Met115）肌动蛋白交联位点周围序列设计的合成十二肽抑制了丝切蛋白与肌动蛋白的结合。此外，发现该十二肽是肌动蛋白聚合的有效抑制剂。因此，我们得出结论，十二肽序列构成了丝切蛋白肌动蛋白结合和解聚活性所必需的区域。在其他肌动蛋白解聚蛋白，如肌动蛋白解聚因子、肌动蛋白解聚因子和去肌动蛋白中发现了与十二肽相似的序列。因此，十二肽序列可能是肌动蛋白解聚蛋白中肌动蛋白结合和解聚活性所必需的共有序列。
