The Leishmania amazonensis TRF (TTAGGG repeat-binding factor) homologue binds and co-localizes with telomeres |
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| Authors: | Marcelo S da Silva Arina M Perez Rita de Cássia V da Silveira Camila E de Moraes Jair L Siqueira-Neto Lucio H Freitas-Junior Maria Isabel N Cano |
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| Affiliation: | 1.Telomeres Laboratory, Department of Genetics, Biosciences Institute,Universidade Estadual Paulista Júlio de Mesquita Filho,UNESP,Botucatu,Brazil;2.Center for Neglected Diseases Drug Discovery (CND3),Institut Pasteur Korea,South Korea |
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| Abstract: | Background Telomeres are specialized structures at the end of chromosomes essential for maintaining genome stability and cell viability. The importance of telomeric proteins for telomere maintenance has increased our interest in the identification of homologues within the genus Leishmania. The mammalian TRF1 and TRF2 proteins, for example, bind double-stranded telomeres via a Myb-like DNA-binding domain and are involved with telomere length regulation and chromosome end protection. In addition, TRF2 can modulate the activity of several enzymes and influence the conformation of telomeric DNA. In this work, we identified and characterized a Leishmania protein (LaTRF) homologous to both mammalian TRF1 and TRF2. |
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