Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/80843
Type: Artigo de periódico
Title: Leishmania replication protein A-1 binds in vivo single-stranded telomeric DNA
Author: Neto, JLS
Lira, CBB
Giardini, MA
Khater, L
Perez, AM
Peroni, LA
dos Reis, JRR
Freitas, LH
Ramos, CHI
Cano, MIN
Abstract: Replication protein A (RPA) is a highly conserved heterotrimeric single-stranded DNA-binding protein involved in different events of DNA metabolism. In yeast, subunits 1 (RPA-1) and 2 (RPA-2) work also as telomerase recruiters and, in humans, the complex unfolds G-quartet structures formed by the 3' G-rich telomeric strand. In most eukaryotes, RPA-1 and RPA-2 bind DNA using multiple OB fold domains. In trypanosomatids, including Leishmania, RPA-1 has a canonical OB fold and a truncated RFA-1 structural domain. In Leishmania amazonensis, RPA-1 alone can form a complex in vitro with the telomeric G-rich strand. In this work, we show that LaRPA-1 is a nuclear protein that associates in vivo with Leishmania telomeres. We mapped the boundaries of the OB fold DNA-binding domain using deletion mutants. Since Leishmania and other trypanosomatids lack homologues of known telomere end binding proteins, our results raise questions about the function of RPA-1 in parasite telomeres. (C) 2007 Elsevier Inc. All rights reserved.
Subject: replication protein A-1
Leishmania amazonensis
OB fold
telomere end binding protein
immunolocalization
Country: EUA
Editor: Academic Press Inc Elsevier Science
Rights: fechado
Identifier DOI: 10.1016/j.bbrc.2007.04.144
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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