| Texto completo | |
| Autor(es): |
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]
Número total de Autores: 7
|
| Afiliação do(s) autor(es): | [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
Número total de Afiliações: 5
|
| Tipo de documento: | Artigo Científico |
| Fonte: | FEBS Letters; v. 588, n. 24, p. 4740-4748, DEC 20 2014. |
| Citações Web of Science: | 6 |
| Resumo | |
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) | |
| Processo FAPESP: | 12/50263-5 - Estudo das interações entre a proteína telomérica RPA-1 de Leishmania amazonensis (LaRPA-1) e suas parceiras na presença e ausência de estresse oxidativo |
| Beneficiário: | Maria Isabel Nogueira Cano |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |