Zaballos A, Salas M
Centro de Biologia Molecular (CSIC-UAM), Universidad Autónoma, Canto Blanco, Madrid, Spain.
Nucleic Acids Res. 1989 Dec 25;17(24):10353-66. doi: 10.1093/nar/17.24.10353.
Deletion mutants at the amino- and carboxyl-ends of the phi 29 terminal protein, as well as internal deletion and substitution mutants, whose ability to prime the initiation of phi 29 DNA replication was affected to different extent, have been assayed for their capacity to interact with DNA or with the phi 29 DNA polymerase. One DNA binding domain at the amino end of the terminal protein has been mapped. Two regions involved in the binding to the DNA polymerase, an internal region near the amino-terminus and a carboxyl-terminal one, have been also identified. Interaction with both DNA and phi 29 DNA polymerase are required to led to the formation of terminal protein-dAMP initiation complex to start phi 29 DNA replication.
对φ29末端蛋白氨基端和羧基端的缺失突变体，以及内部缺失和取代突变体进行了检测，这些突变体引发φ29 DNA复制起始的能力受到不同程度的影响，检测它们与DNA或φ29 DNA聚合酶相互作用的能力。已确定末端蛋白氨基端的一个DNA结合结构域。还鉴定出了与DNA聚合酶结合的两个区域，一个是靠近氨基端的内部区域，另一个是羧基端区域。与DNA和φ29 DNA聚合酶的相互作用都是形成末端蛋白-dAMP起始复合物以启动φ29 DNA复制所必需的。
