Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870039 | FEBS Letters | 2014 | 9 Pages |
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.
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Authors
R.S. Pavani, C. Fernandes, A.M. Perez, E.J.R. Vasconcelos, J.L. Siqueira-Neto, M.R. Fontes, M.I.N. Cano,