Mellado R P, Salas M
Nucleic Acids Res. 1983 Nov 11;11(21):7397-407. doi: 10.1093/nar/11.21.7397.
A mutant at the carboxyl end of the terminal protein, p3, of phage phi 29 DNA has been constructed by inserting an containing the stop translation codon TGA in the three possible reading frames, immediately downstream of a phage phi 29 DNA fragment coding for all but the last five amino acids of protein p3. The activity in the formation of the p3-dAMP initiation complex in vitro of this mutant as well as another one previously isolated, also mutated at the carboxyl end, have been tested. The results obtained suggest that an intact carboxyl end in the phage phi 29 terminal protein is essential for its normal primer function in DNA replication.
通过在噬菌体φ29 DNA片段(编码除p3蛋白最后五个氨基酸外的所有氨基酸)的下游,以三种可能的阅读框插入包含终止翻译密码子TGA的片段,构建了噬菌体φ29 DNA末端蛋白p3羧基端的一个突变体。已经测试了该突变体以及先前分离的另一个在羧基端也发生突变的突变体在体外形成p3-dAMP起始复合物的活性。获得的结果表明,噬菌体φ29末端蛋白完整的羧基端对于其在DNA复制中的正常引物功能至关重要。