Zaballos A, Mellado R P, Salas M
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Gene. 1988;63(1):113-21. doi: 10.1016/0378-1119(88)90550-1.
Series of deletions at the amino end of protein p3, the phage phi 29 DNA terminal protein (TP), have been constructed and characterized. Measurements of the activity of the deletion mutants in the formation of the protein p3-dAMP initiation complex in vitro indicate the dispensability of the first 13 amino acids (aa) of the protein. The activity of protein p3 decreased considerably when 17 or more aa were deleted. The results on the in vitro phi 29 DNA replication primed by the p3 deletion mutants correlated very well with those obtained in the formation of the TP-dAMP initiation complex.
已构建并表征了噬菌体φ29 DNA末端蛋白（TP）p3蛋白氨基末端的一系列缺失。对缺失突变体在体外形成p3-dAMP起始复合物活性的测量表明，该蛋白的前13个氨基酸（aa）是可有可无的。当缺失17个或更多氨基酸时，p3蛋白的活性显著降低。由p3缺失突变体引发的体外φ29 DNA复制结果与在TP-dAMP起始复合物形成中获得的结果非常吻合。
