Yen T S, Webster R E
J Biol Chem. 1981 Nov 10;256(21):11259-65.
We have isolated and characterized the 2 major proteins of a dense complex which accumulate in EScherichia coli cells infected with bacteriophage f1 under conditions where the phage gene V protein is inactive (Webster, R. E., and Rementer, M. (1980) J. Mol. Biol. 139, 393-405). The amino acid composition and NH2- and COOH-terminal sequences of the larger polypeptide (estimated molecular weight of 46,000) correspond to those predicted from the DNA sequence for the f1 gene II protein. The other polypeptide (estimated molecular weight of 14,000) has the amino acid composition and COOH-terminal sequence predicted for the f1 X protein, which previously had been found only as a product of an in vitro transcription-translation reaction. The X protein contains N-formylmethionine, cross-reacts with antibodies against gene II protein, and is present in wild type f1-infected bacteria. Thus, X protein is the product of f1 gene X (10), which is contained entirely in, and translated in phase with, gene II.
我们已经分离并鉴定了一种致密复合物中的两种主要蛋白质,该复合物在噬菌体基因V蛋白无活性的条件下,在感染了噬菌体f1的大肠杆菌细胞中积累(韦伯斯特,R.E.,和雷门特,M.(1980年)《分子生物学杂志》139卷,393 - 405页)。较大多肽(估计分子量为46,000)的氨基酸组成以及氨基末端和羧基末端序列与根据f1基因II蛋白的DNA序列预测的结果相符。另一种多肽(估计分子量为14,000)具有为f1 X蛋白预测的氨基酸组成和羧基末端序列,f1 X蛋白此前仅作为体外转录 - 翻译反应的产物被发现。X蛋白含有N - 甲酰甲硫氨酸,与针对基因II蛋白的抗体发生交叉反应,并且存在于野生型f1感染的细菌中。因此,X蛋白是f1基因X(10)的产物,它完全包含在基因II中并与基因II同相位翻译。