Otero M J, Salas M
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Nucleic Acids Res. 1989 Jun 26;17(12):4567-77. doi: 10.1093/nar/17.12.4567.
Series of deletions corresponding to the carboxyl end of the phage phi 29 protein p6 have been constructed and their activity in the initiation of phi 29 DNA replication and their capacity to interact with the phi 29 DNA ends have been studied. Determination of the activity of the deletion mutants in phi 29 DNA replication indicated the dispensability of the 14 carboxy-terminal amino acids of the protein. The activity of protein p6 decreased with deletions from 23 to 39 amino acids and was undetectable when 44 amino acids were removed. A similar behaviour was obtained when the interaction of the mutant proteins with the phi 29 DNA ends was analyzed. These results indicate that the stimulation of phi 29 DNA replication by protein p6 requires a specific binding to the phi 29 DNA ends.
构建了一系列与噬菌体φ29蛋白p6羧基末端相对应的缺失片段，并研究了它们在启动φ29 DNA复制中的活性以及与φ29 DNA末端相互作用的能力。对缺失突变体在φ29 DNA复制中的活性测定表明，该蛋白的14个羧基末端氨基酸是可有可无的。随着从23到39个氨基酸的缺失，蛋白p6的活性降低，当去除44个氨基酸时则检测不到其活性。在分析突变蛋白与φ29 DNA末端的相互作用时也得到了类似的结果。这些结果表明，蛋白p6对φ29 DNA复制的刺激需要与φ29 DNA末端进行特异性结合。
