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Trax is a component of the Translin-containing RNA binding complex
Patricia M Finkenstadt1, Mihee Jeon, Jay M Baraban
1Department of Neuroscience, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA.
Journal of Neurochemistry
|October 3, 2002
Summary
Translin and Trax form a complex that binds nucleic acids. This study confirms both proteins are part of the native gel-shift complex, regardless of whether DNA or RNA probes are used.
Area of Science:
- Molecular Biology
- Neuroscience
- RNA Biology
Background:
- Translin is a nucleic acid binding protein involved in dendritic RNA targeting and translation.
- Translin and Trax form a gel-shift complex enriched in brain extracts.
- Previous studies used DNA (GS1) and RNA (protamine-2 3' UTR) probes to study this complex.
Purpose of the Study:
- To re-examine the composition of the Translin-containing gel-shift complex.
- To clarify whether the native complex contains Trax, given its RNA binding inhibitory role.
- To determine if DNA and RNA probes label the same complex.
Main Methods:
- Gel-shift assays using DNA (GS1) and RNA (protamine-2) probes.
- Supershift analysis with Trax antibodies.
- Cross-competition studies.
- Analysis of recombinant Translin/Trax complexes via co-transfection.
Main Results:
- Both GS1 and protamine-2 probes labeled heteromeric Translin/Trax complexes, as indicated by supershift with Trax antibodies.
- Cross-competition studies confirmed both probes label the same complex.
- Recombinant Translin/Trax complexes were labeled by both probes.
- Recombinant Translin alone formed a homomeric complex, but the native complex includes Trax.
Conclusions:
- The native gel-shift complex labeled by either DNA or RNA probes consistently contains both Translin and Trax.
- These findings resolve previous ambiguity regarding Trax's role in the native complex.
- The study confirms the heteromeric nature of the Translin/Trax nucleic acid binding complex.