Purification of a functional enzymatic editing complex from Trypanosoma brucei mitochondria

Laura N. Rusché, Jorge Cruz-Reyes, Kenneth J. Piller, Barbara Sollner-Webb

Research output: Contribution to journalArticlepeer-review

142 Scopus citations


Kinetoplastid mitochondrial RNA editing, the insertion and deletion of U residues, is catalyzed by sequential cleavage, U addition or removal, and ligation reactions and is directed by complementary guide RNAs. We have purified a ~20S enzymatic complex from Trypanosoma brucei mitochondria that catalyzes a complete editing reaction in vitro. This complex possesses all four activities predicted to catalyze RNA editing: gRNA-directed endonuclease, terminal uridylyl transferase, 3' U-specific exonuclease, and RNA ligase. However, it does not contain other putative editing complex components: gRNA-independent endonuclease, RNA helicase, endogenous gRNAs or pre-mRNAs, or a 25 kDa gRNA-binding protein. The complex is composed of eight major polypeptides, three of which represent RNA ligase. These findings identify polypeptides representing catalytic editing factors, reveal the nature of this ~20S editing complex, and suggest a new model of editosome assembly.

Original languageEnglish (US)
Pages (from-to)4069-4081
Number of pages13
JournalEMBO Journal
Issue number13
StatePublished - Jul 1 1997


  • Editing complex
  • RNA editing
  • RNA lipase
  • Trypanosoma brucei
  • Trypanosome

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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