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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

RPA-1 from Leishmania amazonensis (LaRPA-1) structurally differs from other eukaryote RPA-1 and interacts with telomeric DNA via its N-terminal OB-fold domain

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Author(s):
Pavani, R. S. [1] ; Fernandes, C. [2] ; Perez, A. M. [3] ; Vasconcelos, E. J. R. [4] ; Siqueira-Neto, J. L. [5] ; Fontes, M. R. [2] ; Cano, M. I. N. [1]
Total Authors: 7
Affiliation:
[1] Univ Estadual Paulista Julio De Mesquita Filho UN, Inst Biociencias, Dept Genet, BR-18618970 Botucatu, SP - Brazil
[2] Univ Estadual Paulista Julio De Mesquita Filho UN, Inst Biociencias, Dept Fis & Biofis, BR-18618970 Botucatu, SP - Brazil
[3] CNPEM, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, SP - Brazil
[4] Seattle Biomed Res Inst, Seattle, WA 98109 - USA
[5] Univ Calif San Diego, Skaggs Sch Pharm & Pharmaceut Sci, La Jolla, CA 92093 - USA
Total Affiliations: 5
Document type: Journal article
Source: FEBS Letters; v. 588, n. 24, p. 4740-4748, DEC 20 2014.
Web of Science Citations: 6
Abstract

Replication protein A-1 (RPA-1) is a single-stranded DNA-binding protein involved in DNA metabolism. We previously demonstrated the interaction between LaRPA-1 and telomeric DNA. Here, we expressed and purified truncated mutants of LaRPA-1 and used circular dichroism measurements and molecular dynamics simulations to demonstrate that the tertiary structure of LaRPA-1 differs from human and yeast RPA-1. LaRPA-1 interacts with telomeric ssDNA via its N-terminal OB-fold domain, whereas RPA from higher eukaryotes show different binding modes to ssDNA. Our results show that LaRPA-1 is evolutionary distinct from other RPA-1 proteins and can potentially be used for targeting trypanosomatid telomeres. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. (AU)