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TitleStructure of the core editing complex (L-complex) involved in uridine insertion/deletion RNA editing in trypanosomatid mitochondria.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 106, Issue 30, Page 12306-12310, Year 2009
Publish dateJul 28, 2009
AuthorsFeng Li / Peng Ge / Wong H Hui / Ivo Atanasov / Kestrel Rogers / Qiang Guo / Daren Osato / Arnold M Falick / Z Hong Zhou / Larry Simpson /
PubMed AbstractUridine insertion/deletion RNA editing is a unique form of posttranscriptional RNA processing that occurs in mitochondria of kinetoplastid protists. We have carried out 3D structural analyses of the ...Uridine insertion/deletion RNA editing is a unique form of posttranscriptional RNA processing that occurs in mitochondria of kinetoplastid protists. We have carried out 3D structural analyses of the core editing complex or "L (ligase)-complex" from Leishmania tarentolae mitochondria isolated by the tandem affinity purification procedure (TAP). The purified material, sedimented at 20-25S, migrated in a blue native gel at 1 MDa and exhibited both precleaved and full-cycle gRNA-mediated U-insertion and U-deletion in vitro activities. The purified L-complex was analyzed by electron tomography to determine the extent of heterogeneity. Three-dimensional structural comparisons of individual particles in the tomograms revealed that a majority of the complexes have a similar shape of a slender triangle. An independent single-particle reconstruction, using a featureless Gaussian ball as the initial model, converged to a similar triangular structure. Another single-particle reconstruction, using the averaged tomography structure as the initial model, yielded a similar structure. The REL1 ligase was localized on the model to the base of the apex by decoration with REL1-specific IgG. This structure should prove useful for a detailed analysis of the editing reaction.
External linksProc Natl Acad Sci U S A / PubMed:19590014 / PubMed Central
MethodsEM (single particle)
Resolution23.0 Å
Structure data

EMDB-5581:
Negatively Stained TEM structure of trypanosomatid core editing complex (L-complex)
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Leishmania major (eukaryote)

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