High affinity binding of the Translin/Trax complex to RNA does not require the presence of Y or H elements

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)123-129
Number of pages7
JournalMolecular Brain Research
Volume120
Issue number2
DOIs
StatePublished - Jan 5 2004

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RNA
Protein Biosynthesis
Mutation
Proteins
protamine 2

Keywords

  • Dendritic RNA
  • Protamine-2
  • RNA binding complex
  • RNA translation
  • Translin
  • Trax

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

Cite this

High affinity binding of the Translin/Trax complex to RNA does not require the presence of Y or H elements. / Li, Zhi; Baraban, Jay M.

In: Molecular Brain Research, Vol. 120, No. 2, 05.01.2004, p. 123-129.

Research output: Contribution to journalArticle

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