Tb(3+)-tRNA for LRET studies of protein synthesis

Bioconjug Chem. 2013 Jul 17;24(7):1186-90. doi: 10.1021/bc400062d. Epub 2013 Jun 17.

Abstract

When suitably labeled bulk tRNAs are transfected into cells they give rise to FRET (fluorescence resonance energy transfer) signals via binding to ribosomes that provide a measure of total protein synthesis. Application of this approach to monitoring rates of specific protein synthesis requires achieving a very high signal-to-noise ratio. Such high ratios may be attainable using LRET (luminescence resonance energy transfer) in place of FRET. Lanthanide complexes containing an antenna chromophore are excellent LRET donors. Here we describe the synthesis of a Phe-tRNA(Phe) labeled with a Tb(3+) complex, denoted Tb(3+)-Phe-tRNA(Phe) that, notwithstanding the bulkiness of the Tb(3+) complex, is active in protein synthesis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Energy Transfer
  • Magnetic Resonance Spectroscopy
  • Protein Biosynthesis*
  • RNA, Transfer / chemistry*
  • Spectrometry, Mass, Electrospray Ionization
  • Terbium / chemistry*

Substances

  • Terbium
  • RNA, Transfer