High affinity binding of the Translin/Trax complex to RNA does not require the presence of Y or H elements.

Translin and its partner protein, Trax, are components of an RNA binding complex that has been implicated in suppressing translation of several mRNAs by binding to Y and H cis elements contained in these transcripts. However, it is unclear which features of these elements are critical for conferring high affinity binding to the Translin/Trax complex, information that might be useful in identifying other candidate transcripts targeted by this complex. To help clarify this issue, we have assessed the effect of truncating or mutating a segment of the 3'UTR of the protamine-2 transcript which contains both Y and H elements and binds to this complex with high affinity. Our results indicate that high affinity binding to this segment is preserved following extensive mutation of the Y and H elements as long as clusters of G residues are retained. Thus, our findings indicate that the Translin/Trax complex recognizes clusters of G residues rather than RNA sequences that closely match the primary sequence of the Y and H elements. This revised view of the cis elements recognized by the Translin/Trax complex may be useful in future studies aimed at identifying endogenous RNA species targeted by this complex.