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Testis-brain RNA-binding protein, a testicular translational regulatory RNA-binding protein, is present in the brain and binds to the 3' untranslated regions of transported brain mRNAs.

Previous studies have demonstrated that a phosphoprotein in testis binds to transcript c, a sequence containing two highly conserved elements, Y and H, in the 3' untranslated region (UTR) of mouse protamine 2 mRNA (mP2) and represses its translation in vitro. When gel-retardation assays were performed with cytoplasmic extracts prepared from seven different mouse tissues, we found that brain in addition to testis contains a protein that binds to transcript c. Both the testis and brain proteins are found exclusively in the nonpolysomal fractions of their postmitochondrial extracts. The testis and brain proteins appear to be identical according to numerous criteria: the complexes they form with transcript c have identical mobility in native gels, identical optimal pH, identical lability to increased salt concentrations, identical chromatographic properties, identical molecular sizes as judged from UV crosslinking, and identical peptide mapping as revealed by V8 digestion of the UV crosslinked protein-RNA complexes. In addition to binding to the same conserved sequence in the 3'UTR of mP2, the phosphoprotein from testis and brain, hereafter called testis-brain RNA-binding protein (TB-RBP), also specifically binds to a similar sequence in the 3'UTR of brain Tau mRNA. Since TB-RBP binds to the 3'UTRs of several translationally regulated mRNAs in testis and since numerous transported brain mRNAs also contain the same conserved binding elements, we propose that TB-RBP plays a role in mRNA storage, translocation, and/or localization in brain and testis.