Baker T A, Mizuuchi M, Mizuuchi K
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
Cell. 1991 Jun 14;65(6):1003-13. doi: 10.1016/0092-8674(91)90552-a.
The MuA and MuB proteins collaborate to mediate efficient transposition of the phage Mu genome into many DNA target sites. MuA (the transposase) carries out all the DNA cleavage and joining steps. MuB stimulates strand transfer by activating the MuA-donor DNA complex through direct protein-protein contact. The C-terminal domain of MuA is required for this MuA-MuB interaction. Activation of strand transfer occurs irrespective of whether MuB is bound to target DNA. When high levels of MuA generate a pool of free MuB (not bound to DNA) or when chemical modification of MuB impairs its ability to bind DNA, MuB still stimulates strand transfer. However, under these conditions, intramolecular target sites are used exclusively because of their close proximity to the MuA-MuB-donor DNA complex.
MuA和MuB蛋白协同作用，介导噬菌体Mu基因组高效转座到许多DNA靶位点。MuA（转座酶）执行所有的DNA切割和连接步骤。MuB通过直接的蛋白质-蛋白质接触激活MuA-供体DNA复合物，从而刺激链转移。MuA的C末端结构域是这种MuA-MuB相互作用所必需的。无论MuB是否与靶DNA结合，链转移都会被激活。当高水平的MuA产生大量游离的MuB（未与DNA结合）时，或者当MuB的化学修饰损害其结合DNA的能力时，MuB仍然会刺激链转移。然而，在这些条件下，由于分子内靶位点与MuA-MuB-供体DNA复合物距离很近，所以只会使用分子内靶位点。
