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.
Aphasizhev
Ruslan
R
Department of Microbiology, Immunology and Molecular Genetics, Howard Hughes Medical Institute, University of California at Los Angeles, Los Angeles, CA 90095, USA.
Aphasizheva
Inna
I
Nelson
Robert E
RE
Gao
Guanghan
G
Simpson
Agda M
AM
Kang
Xuedong
X
Falick
Arnold M
AM
Sbicego
Sandro
S
Simpson
Larry
L
D000595:Amino Acid Sequence; D000818:Animals; D007891:Leishmania / Q000235:genetics* / Q000378:metabolism; D008928:Mitochondria / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D011485:Protein Binding; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017393:RNA Editing; D016415:Sequence Alignment; D014498:Uracil
D015800:Protozoan Proteins; D014498:Uracil