FRET analysis of in vivo dimerization by RNA-editing enzymes

Kaari A. Chilibeck, Tao Wu, Chao Liang, Matthew J. Schellenberg, Emily M. Gesner, Jeffrey M. Lynch, Andrew M. MacMillan

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

Members of the ADAR (adenosine deaminase that acts on RNA) enzyme family catalyze the hydrolytic deamination of adenosine to inosine within double-stranded RNAs, a poorly understood process that is critical to mammalian development. We have performed fluorescence resonance energy transfer experiments in mammalian cells transfected with fluorophore-bearing ADAR1 and ADAR2 fusion proteins to investigate the relationship between these proteins. These studies conclusively demonstrate the homodimerization of ADAR1 and ADAR2 and also show that ADAR1 and ADAR2 form heterodimers in human cells. RNase treatment of cells expressing these fusion proteins changes their localization but does not affect dimerization. Taken together these results suggest that homo- and heterodimerization are important for the activity of ADAR family members in vivo and that these associations are RNA independent.

Original languageEnglish (US)
Pages (from-to)16530-16535
Number of pages6
JournalJournal of Biological Chemistry
Volume281
Issue number24
DOIs
StatePublished - Jun 16 2006

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'FRET analysis of in vivo dimerization by RNA-editing enzymes'. Together they form a unique fingerprint.

Cite this