Replication Protein A‐1 Has a Preference for the Telomeric G‐rich Sequence in Trypanosoma cruzi

Replication protein A (RPA), the major eukaryotic single‐stranded binding protein, is a heterotrimeric complex formed by RPA‐1, RPA‐2, and RPA‐3. RPA is a fundamental player in replication, repair, recombination, and checkpoint signaling. In addition, increasing evidences have been adding functions...

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Bibliographic Details
Published in:The Journal of eukaryotic microbiology 2018-05, Vol.65 (3), p.345-356
Main Authors: Pavani, Raphael Souza, Vitarelli, Marcela O., Fernandes, Carlos A. H., Mattioli, Fabio F., Morone, Mariana, Menezes, Milene C., Fontes, Marcos R. M., Cano, Maria Isabel N., Elias, Maria Carolina
Format: Article
Language:English
Subjects:
Chagas disease
Chagas Disease - parasitology
Chromatin - metabolism
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA damage
DNA replication
DNA, Single-Stranded - genetics
Fish
G‐rich strand
Humans
Nucleotide sequence
Parasites
Protein Binding - genetics
Proteins
Protozoa
Recombination
Replication protein A
Replication Protein A - metabolism
Sequencing
Telomerase
Telomerase - metabolism
Telomere - genetics
Telomere - metabolism
Telomere Homeostasis - physiology
Telomeres
Trypanosoma cruzi
Trypanosoma cruzi - genetics
Trypanosoma cruzi - metabolism
Vector-borne diseases
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Summary:Replication protein A (RPA), the major eukaryotic single‐stranded binding protein, is a heterotrimeric complex formed by RPA‐1, RPA‐2, and RPA‐3. RPA is a fundamental player in replication, repair, recombination, and checkpoint signaling. In addition, increasing evidences have been adding functions to RPA in telomere maintenance, such as interaction with telomerase to facilitate its activity and also involvement in telomere capping in some conditions. Trypanosoma cruzi, the etiological agent of Chagas disease is a protozoa parasite that appears early in the evolution of eukaryotes. Recently, we have showed that T. cruziRPA presents canonical functions being involved with DNA replication and DNA damage response. Here, we found by FISH/IF assays that T. cruziRPA localizes at telomeres even outside replication (S) phase. In vitro analysis showed that one telomeric repeat is sufficient to bind RPA‐1. Telomeric DNA induces different secondary structural modifications on RPA‐1 in comparison with other types of DNA. In addition, RPA‐1 presents a higher affinity for telomeric sequence compared to randomic sequence, suggesting that RPA may play specific roles in T. cruzi telomeric region.
ISSN:1066-5234
1550-7408
DOI:10.1111/jeu.12478