RNA editing-associated protein 1 is an RNA binding protein with specificity for preedited mRNA

Mol Cell. 2001 Apr;7(4):879-86. doi: 10.1016/s1097-2765(01)00231-3.


RNA editing in the mitochondria of kinetoplastids involves the addition and deletion of uridines at specific sites as directed by guide RNAs (gRNAs). Ample evidence shows that ribonucleoprotein (RNP) complexes carry out this posttranscriptional processing. One component of RNA editing complexes is REAP-1, a protein of previously unknown function found primarily in mRNA containing editing complexes. We now show that REAP-1 is an RNA binding protein and map the binding activity to the amino-terminal third of the protein. REAP-1 binds to poly(G) and single-stranded guanosine rich RNAs. Data presented here demonstrates that preedited RNAs are the preferred substrate for REAP-1. The results suggest a model in which the role of REAP-1 is to bring preedited mRNAs into the editing complex.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Base Sequence
  • Binding Sites / genetics
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics*
  • RNA Editing / physiology*
  • RNA, Messenger / metabolism*
  • RNA, Protozoan / metabolism*
  • RNA-Binding Proteins / genetics
  • Trypanosoma brucei brucei / genetics*


  • Protozoan Proteins
  • REAP-1 protein, Trypanosoma brucei
  • RNA, Messenger
  • RNA, Protozoan
  • RNA-Binding Proteins