Vandekerckhove J, Lal A A, Korn E D
J Mol Biol. 1984 Jan 5;172(1):141-7. doi: 10.1016/0022-2836(84)90418-2.
By amino acid sequence studies, only one form of cytoplasmic actin was detected in Acanthamoeba castellanii. Its amino acid sequence is very similar to the sequences of Dictyostelium and Physarum actins, from which Acanthamoeba actin differs in only nine and seven residues, respectively, including the deletion of the first residue. Acanthamoeba actin is unique in containing a blocked NH2-terminal neutral amino acid (glycine), while all other actins sequenced thus far have a blocked acidic amino acid (aspartic or glutamic) at the NH2 terminus. Acanthamoeba actin is also unique in that it contains an N epsilon-trimethyllysine residue at position 326. Like other actins, Acanthamoeba actin contains an NT-methylhistidine residue at position 73. The protein sequence is in complete agreement with the sequence derived from the nucleotide sequence of an expressed actin gene.
通过氨基酸序列研究，在卡氏棘阿米巴中仅检测到一种形式的细胞质肌动蛋白。其氨基酸序列与盘基网柄菌和绒泡菌肌动蛋白的序列非常相似，卡氏棘阿米巴肌动蛋白分别仅在九个和七个残基上与之不同，包括第一个残基的缺失。卡氏棘阿米巴肌动蛋白的独特之处在于其含有一个被封闭的NH2末端中性氨基酸（甘氨酸），而迄今为止测序的所有其他肌动蛋白在NH2末端都含有一个被封闭的酸性氨基酸（天冬氨酸或谷氨酸）。卡氏棘阿米巴肌动蛋白的另一个独特之处在于它在第326位含有一个Nε-三甲基赖氨酸残基。与其他肌动蛋白一样，卡氏棘阿米巴肌动蛋白在第73位含有一个N-甲基组氨酸残基。该蛋白质序列与从一个表达的肌动蛋白基因的核苷酸序列推导的序列完全一致。
