In vitro RNA editing in plant mitochondria does not require added energy

FEBS Lett. 2007 Jun 12;581(14):2743-7. doi: 10.1016/j.febslet.2007.05.025. Epub 2007 May 21.

Abstract

RNA editing in flowering plant mitochondria is investigated by in vitro assays. These cauliflower mitochondrial lysates require added NTP or dNTP. We have now resolved the reason for this requirement to be the inhibition of the RNA binding activity of the glutamate dehydrogenases (GDH). Both GDH1 and GDH2 were identified in RNA-protein cross-links. The inhibition of in vitro RNA editing by GDH is confirmed by the ability of the GDH-specific herbicide phosphinothricin to substitute for NTP. NADH and NADPH, but not NAD or NADP, can also replace NTP, suggesting that the NAD(P)H-binding-pocket configuration of the GDH contacts the RNA. RNA editing in plant mitochondria is thus intrinsically independent of added energy in the form of NTP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Adenosine Triphosphate / pharmacology
  • Aminobutyrates / pharmacology
  • Brassica / genetics*
  • Cytidine Triphosphate / metabolism
  • Cytidine Triphosphate / pharmacology
  • Glutamate Dehydrogenase (NADP+) / antagonists & inhibitors
  • Glutamate Dehydrogenase (NADP+) / metabolism
  • Glutamate Dehydrogenase / antagonists & inhibitors
  • Glutamate Dehydrogenase / metabolism
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / metabolism
  • Mitochondria / drug effects
  • Mitochondria / genetics*
  • Mitochondria / metabolism
  • Mitochondrial Proteins / metabolism
  • Mitochondrial Proton-Translocating ATPases / genetics
  • NAD / metabolism
  • NAD / pharmacology
  • Protein Binding
  • RNA / genetics*
  • RNA / metabolism
  • RNA Editing*
  • RNA, Mitochondrial
  • Reverse Transcriptase Polymerase Chain Reaction

Substances

  • Aminobutyrates
  • Isoenzymes
  • Mitochondrial Proteins
  • RNA, Mitochondrial
  • NAD
  • phosphinothricin
  • RNA
  • Cytidine Triphosphate
  • Adenosine Triphosphate
  • Glutamate Dehydrogenase
  • Glutamate Dehydrogenase (NADP+)
  • Mitochondrial Proton-Translocating ATPases