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Title: LaRbp38: A Leishmania amazonensis protein that binds nuclear and kinetoplast DNAs

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.

Authors:
 [1];  [1];  [1];  [2];  [3];  [1]
  1. Departamento de Genetica, IB, Universidade Estadual de Sao Paulo, UNESP, 18618-000, Botucatu, SP (Brazil)
  2. Instituto de Biologia, UNICAMP, Campinas, SP (Brazil)
  3. Instituto de Quimica, UNICAMP, Campinas, SP (Brazil)
Publication Date:
OSTI Identifier:
20991430
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 358; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2007.05.005; PII: S0006-291X(07)00955-2; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CHROMATIN; CHROMATOGRAPHY; DNA; DRUGS; IN VIVO; MASS SPECTROSCOPY; MITOCHONDRIA; POLYPEPTIDES; PURIFICATION; RNA

Citation Formats

Lira, C B.B., Instituto de Biologia, UNICAMP, Campinas, SP, Siqueira Neto, J L, Instituto de Biologia, UNICAMP, Campinas, SP, Giardini, M A, Instituto de Biologia, UNICAMP, Campinas, SP, Winck, F V, Ramos, C H.I., and Cano, M I.N. . LaRbp38: A Leishmania amazonensis protein that binds nuclear and kinetoplast DNAs. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.05.005.
Lira, C B.B., Instituto de Biologia, UNICAMP, Campinas, SP, Siqueira Neto, J L, Instituto de Biologia, UNICAMP, Campinas, SP, Giardini, M A, Instituto de Biologia, UNICAMP, Campinas, SP, Winck, F V, Ramos, C H.I., & Cano, M I.N. . LaRbp38: A Leishmania amazonensis protein that binds nuclear and kinetoplast DNAs. United States. https://doi.org/10.1016/j.bbrc.2007.05.005
Lira, C B.B., Instituto de Biologia, UNICAMP, Campinas, SP, Siqueira Neto, J L, Instituto de Biologia, UNICAMP, Campinas, SP, Giardini, M A, Instituto de Biologia, UNICAMP, Campinas, SP, Winck, F V, Ramos, C H.I., and Cano, M I.N. . 2007. "LaRbp38: A Leishmania amazonensis protein that binds nuclear and kinetoplast DNAs". United States. https://doi.org/10.1016/j.bbrc.2007.05.005.
@article{osti_20991430,
title = {LaRbp38: A Leishmania amazonensis protein that binds nuclear and kinetoplast DNAs},
author = {Lira, C B.B. and Instituto de Biologia, UNICAMP, Campinas, SP and Siqueira Neto, J L and Instituto de Biologia, UNICAMP, Campinas, SP and Giardini, M A and Instituto de Biologia, UNICAMP, Campinas, SP and Winck, F V and Ramos, C H.I. and Cano, M I.N. .},
abstractNote = {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.},
doi = {10.1016/j.bbrc.2007.05.005},
url = {https://www.osti.gov/biblio/20991430}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 358,
place = {United States},
year = {Fri Jul 06 00:00:00 EDT 2007},
month = {Fri Jul 06 00:00:00 EDT 2007}
}