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Leishmania replication protein A-1 binds in vivo single-stranded telomeric DNA

2007; Elsevier BV; Volume: 358; Issue: 2 Linguagem: Inglês

10.1016/j.bbrc.2007.04.144

1090-2104

Jair L. Siqueira-Neto, C.B.B. Lira, Miriam A. Giardini, Letícia Khater, Alessandra Maia Marques Martinez Perez, L Peroni, José Raimundo Ribeiro dos Reis, Lúcio H. Freitas-Júnior, Carlos H.I. Ramos, Maria Isabel Nogueira Cano,

CRISPR and Genetic Engineering

Replication protein A (RPA) is a highly conserved heterotrimeric single-stranded DNA-binding protein involved in different events of DNA metabolism. In yeast, subunits 1 (RPA-1) and 2 (RPA-2) work also as telomerase recruiters and, in humans, the complex unfolds G-quartet structures formed by the 3' G-rich telomeric strand. In most eukaryotes, RPA-1 and RPA-2 bind DNA using multiple OB fold domains. In trypanosomatids, including Leishmania, RPA-1 has a canonical OB fold and a truncated RFA-1 structural domain. In Leishmania amazonensis, RPA-1 alone can form a complex in vitro with the telomeric G-rich strand. In this work, we show that LaRPA-1 is a nuclear protein that associates in vivo with Leishmania telomeres. We mapped the boundaries of the OB fold DNA-binding domain using deletion mutants. Since Leishmania and other trypanosomatids lack homologues of known telomere end binding proteins, our results raise questions about the function of RPA-1 in parasite telomeres.