Binding of U1A protein to the 3' untranslated region of its pre-mRNA

Richard J. Grainger, David G. Norman, David M.J. Lilley

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

We have studied the global structure of the U1A 3' untranslated region (UTR) element using fluorescence resonance energy transfer. Comparison of a single UTR-box with a series of oligoadenine bulges indicates that the UTR-box introduces a significant kink into the axis of the RNA, and quantification of the results suggests an included bend angle of approximately 100°(i.e. 80°from linear). The complete 3' UTR element is also severely kinked by the two UTR-boxes. We can observe binding of U1A protein to the 3'-UTR element by a change in the fluorescence anisotropy of Cy3 attached to one of the helical ends. In parallel with the binding, we observe a marked increase in fluoresence resonance energy transfer efficiency between fluorophores attached at the two 5' termini, indicating a significant change in global conformation induced by the binding of the protein.

Original languageEnglish
Pages (from-to)585-594
Number of pages10
JournalJournal of Molecular Biology
Volume288
Issue number4
DOIs
Publication statusPublished - 14 May 1999

Keywords

  • Fluorescence resonance energy transfer
  • RNA splicing
  • RNA-protein interaction

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