Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/61115
Type: Artigo de periódico
Title: LaRbp38: A Leishmania amazonensis protein that binds nuclear and kinetoplast DNAs
Author: Lira, CBB
Siqueira Neto, JL
Giardini, MA
Winck, FV
Ramos, CHI
Cano, MIN
Abstract: Leishmania amazonensis causes a wide spectrum of leishmaniasis. There are no vaccines or adequate treatment for leishmaniasis, therefore there is considerable interest in the identification of new targets for anti-leishmania drugs. The central role of telomere-binding proteins in cell maintenance makes these proteins potential targets for new drugs. In this work, we used a combination of purification chromatographies to screen L. amazonensis proteins for molecules capable of binding double-stranded telomeric DNA. This approach resulted in the purification of a 38 kDa polypeptide that was identified by mass spectrometry as Rbp38, a trypanosomatid protein previously shown to stabilize mitochondrial RNA and to associate with nuclear and kinetoplast DNAs. Western blotting and supershift assays confirmed the identity of the protein as LaRbp38. Competition and chromatin immunoprecipitation assays confirmed that LaRbp38 interacted with kinetoplast and nuclear DNAs in vivo and suggested that LaRbp38 may have dual cellular localization and more than one function. (C) 2007 Elsevier Inc. All rights reserved.
Subject: GT-rich DNA
kinetoplast DNA
Leishmania amazonensis
Rbp38
telornere-binding protein
Country: EUA
Editor: Academic Press Inc Elsevier Science
Rights: fechado
Identifier DOI: 10.1016/j.bbrc.2007.05.005
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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