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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
Author(s) -
Pavani R.S.,
Fernandes C.,
Perez A.M.,
Vasconcelos E.J.R.,
Siqueira-Neto J.L.,
Fontes M.R.,
Cano M.I.N.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.005
Subject(s) - eukaryote , dna , chemistry , fold (higher order function) , terminal (telecommunication) , biophysics , biology , microbiology and biotechnology , biochemistry , genome , computer science , gene , telecommunications , programming language
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.