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. 2011 Mar 10;6(3):e17701. doi: 10.1371/journal.pone.0017701

Table 2. Y2H-derived PPI data confirmed by alternative and supplementary experimental methods.

Interactor A Interactor B Y2H GST/His-Tag pull-down Biochemical activation Motif mapping Surface plasmon resonance
Imp3 Mpp10 [46] [46] [46]
Imp4 Mpp10 [46] [46] [46]
Esf2 Dbp8 [43] [43] [43]
Pfa1 Prp43 [48], [89] [89] [89] [89]
t-Utp8 t-Utp9 [39], [44] [44] [44] [44]
Utp6 Utp21 [38] [38] [38]
Utp6 Utp18 [38] [38]
Utp25 Utp3 [41], [51] [41] [41], [51]

Many PPIs from the LC data have alternative forms of supporting evidence from experiments that test for binary interactions, including pull-downs, activation of enzymatic activities, motif mapping by truncations and surface plasmon resonance. This list of protein-protein interactions identified by Y2H and validated by independent methods is not exhaustive.