Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/101804
Type: Artigo de periódico
Title: A Trypanosoma Brucei Protein Complex That Binds G-overhangs And Co-purifies With Telomerase Activity
Author: Cano M.I.N.
Blake J.J.
Blackburn E.H.
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.
Editor: 
Rights: fechado
Identifier DOI: 10.1074/jbc.M104111200
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037059811&partnerID=40&md5=aebf0b1278216527153cc67a04a973b3
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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