Leishmania replication protein A-1 binds in vivo single-stranded telomeric DNA
- Departamento de Genetica, Instituto de Biociencias, Universidade Estadual de Sao Paulo, UNESP, 18618-000 Botucatu, SP (Brazil)
- Instituto de Biologia, UNICAMP, Campinas, SP (Brazil)
- Systems Biology of Pathogen, Institut Pasteur Korea, Seoul Korea (Korea, Republic of)
- Instituto de Quimica, UNICAMP, Campinas, SP (Brazil)
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.
- OSTI ID:
- 20991406
- Journal Information:
- Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 358; ISSN 0006-291X; ISSN BBRCA9
- Country of Publication:
- United States
- Language:
- English
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