Trax is a component of the Translin‐containing RNA binding complex

Abstract

Translin is a nucleic acid binding protein that has been implicated in regulating the targeting and translation of dendritic RNA. In previous studies, we found that Translin and its partner protein, Trax, are components of a gel-shift complex that is highly enriched in brain extracts. In those studies, we employed a DNA oligonucleotide, GS1, as a probe to label the complex. Translin has also been identified as a component of a gel-shift complex detected using an RNA oligonucleotide probe, derived from the 3¢ UTR of protamine-2 mRNA. Although we had assumed that these probes labeled the same complex, recent studies indicate that association of Trax with Translin suppresses its RNA binding activity. As these findings challenge this assumption and suggest that the native RNA binding complex does not contain Trax, we have re-examined this issue. We have found that the gel-shift complexes labeled with either GS1 or protamine-2 probes are 'supershifted' by addition of Trax antibodies, indicating that both are heteromeric Translin/Trax complexes. In addition, cross-competition studies provide additional evidence that these probes label the same complex. Furthermore, analysis of recombinant Translin/Trax complexes generated by co-transfection of Trax with Translin in hEK293T demonstrates that they are labeled with either probe. Although recombinant Translin forms a homomeric nucleic acid binding complex in vitro, our findings indicate that both Trax and Translin are components of the native gel-shift complex labeled with either GS1 or protamine-2 probes.

Cloning and characterization of the Schizosaccharomyces pombe homologs of the human protein Translin and the Translin-associated protein TRAX

“…This co-evolution of the two genes suggests that Translin and TRAX are functionally related. We have shown in this study that the S.pombe Translin specifically interacts with the S.pombe TRAX, as was previously observed in studies of the human and the mouse Translins (13,15,42). This observation supports the notion that in S.pombe cells, as well as in human and mouse cells, the two proteins are engaged as a complex in a common metabolic pathway.…”

Structural basis for single-stranded RNA recognition and cleavage by C3PO

“…Tsn and Trax are highly conserved and coexist in many eukaryotes (3–6), including fission yeast, Drosophila melanogaster ( Drosophila ) and animals. They are involved in many important biological processes, such as normal cell growth, genome stability maintenance, neuronal development, spermatogenesis, RNA trafficking and RNA metabolism (7–11).…”

Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: a combined molecular genetics and bioinformatics study

“…TRAX is a Translin paralog, which does not bind nucleic acids. However, it forms specific complexes with Translin (8) and these complexes may also bind nucleic acids (9,10). …”