Molecular and Cellular Biology, October 2001, p. 6833-6840, Vol. 21, No. 20
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.20.6833-6840.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


Seattle Biomedical Research Institute, Seattle, Washington 981091; Departments of Pathobiology2 and Molecular Biotechnology,3 University of Washington, Seattle, Washington 98195; and The Institute for Systems Biology, Seattle, Washington 981054
Received 16 May 2001/Returned for modification 28 June 2001/Accepted 16 July 2001
RNA editing in kinetoplastid mitochondria occurs by a series of enzymatic steps that is catalyzed by a macromolecular complex. Four novel proteins and their corresponding genes were identified by mass spectrometric analysis of purified editing complexes from Trypanosoma brucei. These four proteins, TbMP81, TbMP63, TbMP42, and TbMP18, contain conserved sequences to various degrees. All four proteins have sequence similarity in the C terminus; TbMP18 has considerable sequence similarity to the C-terminal region of TbMP42, and TbMP81, TbMP63, and TbMP42 contain zinc finger motif(s). Monoclonal antibodies that are specific for TbMP63 and TbMP42 immunoprecipitate in vitro RNA editing activities. The proteins are present in the immunoprecipitates and sediment at 20S along with the in vitro editing, and RNA editing ligases TbMP52 and TbMP48. Recombinant TbMP63 and TbMP52 coimmunoprecipitate. These results indicate that these four proteins are components of the RNA editing complex and that TbMP63 and TbMP52 can interact.
Present address: Department of Cell Biology, Harvard Medical
School, Boston, MA 02115.
Present address: CompleGen Inc., Seattle, WA 98104.
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