| Autor: |
Vanhamme, Luc, Perez-Morga, David, Marchal, Christian, Speijer, Dave, Lambert, Laurence, Geuskens, Maurice, Alexandre, Sylvie, Ismaı̈li, Naı̈ma, Göringer, Ulrich, Benne, Rob, Pays, Etienne |
| Zdroj: |
Journal of Biological Chemistry; August 1998, Vol. 273 Issue: 34 p21825-21833, 9p |
| Abstrakt: |
We report the characterization of aTrypanosoma brucei75-kDa protein of the RGG (Arg-Gly-Gly) type, termed TBRGG1. Dicistronic and monocistronic transcripts of theTBRGG1gene were produced by both alternative splicing and polyadenylation. TBRGG1 was found in two or three forms that differ in their electrophoretic mobility on SDS-polyacrylamide gel electrophoresis gels, one of which was more abundant in the procyclic form of the parasite. TBRGG1 was localized to the mitochondrion and appeared to be more abundant in bloodstream intermediate and stumpy forms in which the mitochondrion reactivates and during the procyclic stage, which possesses a fully functional mitochondrion. This protein was characterized to display oligo(U) binding characteristics and was found to co-localize with an in vitroRNA editing activity in a sedimentation analysis. TBRGG1 most likely corresponds to the 83-kDa oligo(U)-binding protein previously identified by UV cross-linking of guide RNA to mitochondrial lysates (Leegwater, P., Speijer, D., and Benne, R. (1995) Eur. J. Biochem.227, 780–786). |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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