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Isolation of a U‐insertion/deletion editing complex from Leishmania tarentolae mitochondria

A multiprotein, high molecular weight complex active in both U‐insertion and U‐deletion as judged by a pre‐cleaved RNA editing assay was isolated from mitochondrial extracts of Leishmania tarentolae by the tandem affinity purification (TAP) procedure, using three different TAP‐tagged proteins of the complex. This editing‐ or E‐complex consists of at least three protein‐containing components interacting via RNA: the RNA ligase‐containing L‐complex, a 3′ TUTase (terminal uridylyltransferase) and two RNA‐binding proteins, Ltp26 and Ltp28. Thirteen approximately stoichiometric components were identified by mass spectrometric analysis of the core L‐complex: two RNA ligases; homologs of the four Trypanosoma brucei editing proteins; and seven novel polypeptides, among which were two with RNase III, one with an AP endo/exonuclease and one with nucleotidyltransferase motifs. Three proteins have no similarities beyond kinetoplastids.