Schuck Stephen, Stenlund Arne
Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.
J Virol. 2006 Aug;80(15):7491-9. doi: 10.1128/JVI.00435-06.
The E1 protein from papillomaviruses is a multifunctional protein with complex functions required for the initiation of viral DNA replication. We have performed a surface mutagenesis of the well-characterized E1 DNA binding domain (DBD). We demonstrate that substitutions of multiple residues on the surface of the E1 DBD are defective for DNA replication without affecting the DNA binding activity of the protein. The defects of individual substitutions include failure to form the double trimer that melts the ori and failure to form the double hexamer that unwinds the ori. These results demonstrate that the DBD plays an essential role in multiple DNA replication-related processes apart from DNA binding.
乳头瘤病毒的E1蛋白是一种多功能蛋白,在病毒DNA复制起始过程中具有复杂功能。我们对已充分表征的E1 DNA结合结构域(DBD)进行了表面诱变。我们证明,E1 DBD表面多个残基的取代对DNA复制有缺陷,但不影响该蛋白的DNA结合活性。单个取代的缺陷包括无法形成解开起始位点的双三聚体以及无法形成解开起始位点的双六聚体。这些结果表明,DBD除了DNA结合外,在多个与DNA复制相关的过程中也起着至关重要的作用。