Against the odds, studies with Plk1 PBD revealed that a small and specific phosphopeptide is sufficient for interacting with Plk1 PBD, but not with PBDs from Plk2 or Plk3, with a high affinity (Elia et al. 2003; Yun et al. 2009), suggesting that specific inhibition of Plk1 PBD could be achieved by low-molecular weight, peptide-derived inhibitors, or structurally related compounds.
Like the interaction between human XRCC4 and LigIV (Critchlow et al. 1997), and the interaction between S. cerevisiae Lif1 and Dnl4 (Herrmann et al. 1998), a C-terminal fragment of Lig4 (amino acids 660 913), which contains two BRCT domains, is sufficient for interacting with Xrc4.
To determine whether this region of Uls1 was sufficient for interacting with Slx5, the Uls1531 897 fragment and a partially overlapping fragment (Uls1554-955) that lacks the purported SIM at amino acids 543 551 (Uzunova et al. 2007) were tested in the two-hybrid system.
Combined, these results indicated that a region located between the Uls1 SIMs and ATPase domain was required and sufficient to interact with Slx5 in vivo and that the Uls1-Slx5 interaction did not require binding of Uls1 or Slx5 to SUMO.
In the present study we determine that, although smaller fractions of this region are sufficient to interact with RNMT and stabilize the protein, the first 45 amino acids of RAM are necessary and sufficient to activate RNMT.
We also suggest that administrative affairs alone would not be sufficient to interact and integrate each management purpose.
A single metal is sufficient to interact with the enzyme through the formation of a productive MnATP-enzyme complex, while free ATP inhibits activity.
Thus, adducin tail domains alone are sufficient to interact with F-actin and a single spectrin and to recruit additional spectrin molecules to the ternary complex.
A minimal ATRX fragment consisting of residues 1,260 1,289 was both necessary and sufficient to interact with DAXXDHB (Fig. S1B and S1C).
It may be presumed that at lower loading, the amount of epoxy groups may not be sufficient to interact with the polar silica filler.
