Structure of the mitochondrial editosome-like complex associated TUTase 1 reveals divergent mechanisms of UTP selection and domain organization.

@article{Stagno2010StructureOT,
  title={Structure of the mitochondrial editosome-like complex associated TUTase 1 reveals divergent mechanisms of UTP selection and domain organization.},
  author={Jason R. Stagno and Inna Aphasizheva and Jessica G H Bruystens and Hartmut Luecke and Ruslan Aphasizhev},
  journal={Journal of molecular biology},
  year={2010},
  volume={399 3},
  pages={464-75}
}
RNA uridylylation reactions catalyzed by terminal uridylyl transferases (TUTases) play critical roles in the formation of the mitochondrial transcriptome in trypanosomes. Two mitochondrial RNA editing TUTases have been described: RNA editing TUTase 1 catalyzes guide RNA, ribosomal RNA, and mRNA 3'-uridylylation, and RNA editing TUTase 2 acts as a subunit of the RNA editing core complex (also referred to as the 20S editosome) to perform guided U-insertion mRNA editing. Although RNA editing… CONTINUE READING
Highly Cited
This paper has 21 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 46 references

Identification and characterization of nuclear †http://www.pymol.org non-canonical poly(A) polymerases from Trypanosoma brucei

  • R. D. Etheridge, D. M. Clemens, R. Aphasizhev
  • Mol. Biochem. Parasitol
  • 2009

Similar Papers

Loading similar papers…