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elegans , both FBF proteins physically interact with CPB-1, a cytoplasmic polyadenylation element binding protein ( in vitro selection, high-throughput sequencing of RNA, and sequence specificity landscapes), analysis of RNA-binding preference of FBF-2 PUF domain bound to a 150-amino-acid LST-1 fragment containing one of FBF-binding sites revealed a distinct RNA-binding specificity of the FBF-2/LST-1 complex ( in vitro selection showed that FBF-2 PUF domain changes its RNA-binding mode to 1:1 association of PUM repeats R4-R5 with GA in positions four and five ( FIGURE 3 (B) FBF PUF domains RNA-binding specificity can be influenced by interactions with protein partners such as CPB-1 ( (C) FBFs can repress target mRNAs by recruiting deadenylase complex ( (D) FBFs can promote mRNA polyadenylation by interacting with the poly(A) polymerase complex ( Protein Cofactors That Change PUF Regulatory Outcome Pumilio and FBF proteins lack enzymatic activity and often mediate their regulatory influence by recruiting specific cofactors to their target mRNAs (Wreden et al., 1997