title: High affinity binding of the Translin/Trax complex to RNA does not require the presence of Y or H elements.
abstract: 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.
authors.affiliation: Department of Neuroscience and Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Zhi
authors.initials: Z
authors.lastname: Li
authors.forename: Jay M
authors.initials: JM
authors.lastname: Baraban
mesh_terms: D020413:3' Untranslated Regions / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002540:Cerebral Cortex / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D024202:Electrophoretic Mobility Shift Assay / Q000379:methods; D004622:Embryo, Mammalian; D006801:Humans; D007668:Kidney; D009154:Mutation; D009687:Nuclear Proteins / Q000378:metabolism*; D009841:Oligonucleotides / Q000493:pharmacokinetics; D011479:Protamines / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism; D020218:Response Elements / Q000502:physiology*; D014162:Transfection / Q000379:methods
chemical_list: D020413:3' Untranslated Regions; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D009841:Oligonucleotides; D011479:Protamines; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; C095563:TSN protein, human; C498305:TSNAX protein, human; C498304:Tsn protein, rat; C498307:Tsnax protein, rat; C068621:protamine 2; D012313:RNA