• Neto J L Siqueira
• Lira C B B
• Giardini M A
• Khater L
• Perez A M
• Peroni L A
• dos Reis J R R
• Freitas-Junior L H
• Ramos C H I
• Cano M I N

Biochemical and biophysical research communications

• Publish Date: Jun 2007
• ISSN: 0006-291X
• Volume: 358
• Issue: 2
• Pages: 417-23
• Medium: Print
• Language: English
• Citation (JAMA): Neto J L Siqueira, Lira C B B, Giardini M A, et al. Leishmania Replication Protein A-1 Binds in Vivo Single-stranded Telomeric Dna.. Biochem. Biophys. Res. Commun. Jun 2007;358:417-23

Abstract

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.

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