Trypanosoma brucei gBP21

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منابع مشابه

Association of guide RNA binding protein gBP21 with active RNA editing complexes in Trypanosoma brucei.

RNA editing in Trypanosoma brucei mitochondria produces mature mRNAs by a series of enzyme-catalyzed reactions that specifically insert or delete uridylates in association with a macromolecular complex. Using a mitochondrial fraction enriched for in vitro RNA editing activity, we produced several monoclonal antibodies that are specific for a 21-kDa guide RNA (gRNA) binding protein initially ide...

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Protein synthesis in Trypanosoma brucei brucei was rapidly inhibited during polyamine depletion by DL-adifluoromethylornithine (DFMO) in vitro and in vivo. [3H]Leucine incorporation was depressed 30-40 % by 24 h and 80-90 % by 48 h of DFMO treatment. Concomitantly there was an apparent decrease in the synthesis of the variant-specific glycoprotein (VSG) in DFMO-treated trypanosomes, as measured...

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Protein isoprenylation in Trypanosoma brucei brucei.

Trypanosoma brucei is a digenetic protozoan parasite presenting a public health hazard in certain areas of Africa; it is transmitted between mammals (bloodstream form (BSF)) by tsetse flies (procyclic form (PCF)). We have an ongoing interest in small GTP proteins in T. brucei, and these are commonly isoprenylated. Many isoprenylated proteins belong to the rab family and include ras; the isopren...

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SUMOylation in Trypanosoma brucei

Small ubiquitin like modifier (SUMO) proteins are involved in many processes in eukaryotes. We here show that Trypanosoma brucei SUMO (Tb927.5.3210) modifies many proteins. The levels of SUMOylation were unaffected by temperature changes but were increased by severe oxidative stress. We obtained evidence that trypanosome homologues of the SUMO conjugating enzyme Ubc9 (Tb927.2.2460) and the SUMO...

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Histone modifications in Trypanosoma brucei.

Several biological processes in Trypanosoma brucei are affected by chromatin structure, including gene expression, cell cycle regulation, and life-cycle stage differentiation. In Saccharomyces cerevisiae and other organisms, chromatin structure is dependent upon posttranslational modifications of histones, which have been mapped in detail. The tails of the four core histones of T. brucei are hi...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1997

ISSN: 0021-9258

DOI: 10.1074/jbc.272.6.3749