Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/53942
Type: Artigo de periódico
Title: A Trypanosoma brucei protein complex that binds G-overhangs and co-purifies with telomerase activity.
Author: Cano, MIN
Blake, JJ
Blackburn, EH
Agabian, N
Abstract: The chromosomal ends of Trypanosoma brucei, like those of most eukaryotes, contain conserved 5'-TTAGGG-3' repeated sequences and are maintained by the action of telomerase. Fractionated T. brucei cell extracts with telomerase activity were used as a source of potential regulatory factors or telomerase-associated components that might interact with T. brucei telomeres. Electrophoretic mobility shift assays and UV cross-linking were used to detect possible single-stranded telomeric protein-DNA complexes and to estimate the approximate size of the protein constituents. Three single-stranded telomeric protein-DNA complexes were observed. Complex C3 was highly specific for the G-strand telomeric repeat sequence and shares biochemical characteristics with G-rich, single-stranded telomeric binding proteins and with components of the telomerase holoenzyme described in yeast, ciliates, and humans. Susceptibility to RNase A or chemical nuclease (hydroxyl radical) pre-treatment showed that complex C3 was tightly associated with an RNA component. Matrix-assisted laser desorption/ionization-time of flight mass spectrometry was used to estimate the molecular mass of the peptides obtained by in-gel Lys-C digestion of low abundance C3-associated proteins. The molecular masses of the peptides showed no homologies with other proteins from trypanosomes or with any protein in the data bases screened.
Country: EUA
Editor: Amer Soc Biochemistry Molecular Biology Inc
Rights: fechado
Identifier DOI: 10.1074/jbc.M104111200
Date Issue: 2002
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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