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The Mu A protein is a 75 kDa transposase organized into three structural domains. By severing the C-terminal region (domain III) from the remainder of the protein, we unmasked a novel non-specific DNA binding and nuclease activity in this region. Deletion analysis localized both activities to a 26 amino acid stretch (aa 575-600) which remarkably remained(More)
In a search for Polo-like kinase 1 (Plk1) interaction proteins, we have identified TRF1 (telomeric repeat binding factor 1) as a potential Plk1 target. In this communication we report further characterization of the interaction. We show that Plk1 associates with TRF1, and Plk1 phosphorylates TRF1 at Ser-435 in vivo. Moreover, Cdk1, serving as a priming(More)
  • Z Wu, Xiaoqi Liu
  • Proceedings of the National Academy of Sciences…
  • 2008
In a search for Polo-like kinase 1 (Plk1)-interacting proteins using a yeast two-hybrid system, we have identified histone acetyltransferase binding to the origin recognition complex 1 (Hbo1) as a potential Plk1 target. Here, we show that the interaction between Plk1 and Hbo1 is mitosis-specific and that Plk1 phosphorylates Hbo1 on Ser-57 in vitro and in(More)
Mu A protein, the 75-kDa phage transposase, consists of three domains: a 30-kDa NH2 terminus, a 35-kDa central domain, and a 10-kDa COOH terminus (Nakayama, C., Teplow, D. B., and Harshey, R. M. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 1809-1813). Genetic and biochemical experiments have demonstrated that the COOH-terminal domain must be present for(More)
A series of point mutations was constructed in domain IIIalpha of the Mu A protein. The mutant transposases were purified and assayed for their ability to promote various aspects of the in vitro Mu DNA strand transfer reaction. All mutants with discernable phenotypes were inhibited in stable synapsis (Type 0 or Type 1 complex formation). In contrast, these(More)
A tetramer of the Mu transposase is the structural and functional core in all three stable higher-order nucleoprotein complexes (Type 0, Type 1 and Type 2 transpososomes) generated in a defined in vitro strand transfer reaction. Although functional in donor cleavage, we report here that contrary to previous belief, the Mu A tetramer is incapable of(More)
The effect of flanking host sequences on the cleavage step of the in vitro Mu DNA strand transfer reaction was investigated. Insertion of a mini-Mu molecule into certain sites in pUC19 results in insertions that demonstrate a decreased ability to form Type 1 complexes in subsequent rounds of transposition. Similarly, changes in the flanking host sequences(More)
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