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The Testis Brain RNA-Binding Protein (TB-RBP/ Translin) is a DNA and RNA binding protein with multiple functions. As an RNA-binding protein, TB-RBP binds to conserved sequence elements often present in the 3' UTRs of specific mRNAs modulating their translation and transport. To identify additional mRNA targets of TB-RBP, immunoprecipitation and RT-PCR assays were carried out using an affinity-purified antibody to TB-RBP with testicular extracts. Gapds mRNA was found to be selectively precipitated in a TB-RBP-mRNA complex. Consistent with the delayed translation of GAPDS and the subcellular ribonucleoprotein location of TB-RBP, polysomal gradient analysis showed that most of the Gapds mRNA in adult testis extracts was present in the non-polysomal fractions. In vitro translation assays revealed that Gapds mRNA translation was inhibited by recombinant TB-RBP or by a TB-RBP mutant protein, Nb, capable of binding RNA. No inhibition was seen with mutant forms of TB-RBP lacking domains required for RNA binding, including the TB-RBP Cb mutant and the C-terminal-truncated form of TB-RBP that disrupts the leucine zipper. As an additional indicator of the specificity of TB-RBP inhibition of Gapds mRNA translation, a putative TB-RBP binding H-element was deleted from the 5' UTR of the Gapds mRNA. No translational inhibition by recombinant TB-RBP was seen with Gapds mRNA lacking the H element. These data suggest that TB-RBP is involved in the post-transcriptional regulation of Gapds gene expression during spermiogenes is. Moreover, the Gapds mRNA is the first mRNA shown to have a functional TB-RBP binding site in its 5' UTR.
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