Pennica D, Goeddel D V, Hayflick J S, Reich N C, Anderson C W, Levine A J
Virology. 1984 Apr 30;134(2):477-82. doi: 10.1016/0042-6822(84)90316-7.
A c-DNA clone containing the complete sequence information for the murine p53 protein, from embryonal carcinoma cells, has been isolated. The nucleotide sequence of this clone reveals an open reading frame encoding a protein of 390 amino acids with a molecular weight of 43,364 Da. The NH2-terminal domain of this protein is acidic whereas the carboxyl terminus is rich in basic amino acid residues. These terminal domains are separated by a proline-rich, hydrophobic run of amino acids. Proline comprises approximately 10% of the total amino acid residues. Two tryptic peptides, derived from p53 protein radiolabeled with either methionine or proline, were purified and the position of these labeled residues in the peptide was determined. The positions of three methionine and five proline residues in these two peptides matched the amino acid sequence of the predicted open reading frame determined from the c-DNA clone.
已从胚胎癌细胞中分离出一个包含鼠源p53蛋白完整序列信息的cDNA克隆。该克隆的核苷酸序列揭示了一个开放阅读框，编码一种由390个氨基酸组成、分子量为43,364道尔顿的蛋白质。该蛋白的氨基末端结构域呈酸性，而羧基末端富含碱性氨基酸残基。这些末端结构域被一段富含脯氨酸的疏水氨基酸序列隔开。脯氨酸约占总氨基酸残基的10%。纯化了两条分别用甲硫氨酸或脯氨酸进行放射性标记的源自p53蛋白的胰蛋白酶肽段，并确定了这些标记残基在肽段中的位置。这两条肽段中三个甲硫氨酸残基和五个脯氨酸残基的位置与根据cDNA克隆确定的预测开放阅读框的氨基酸序列相符。
