LaTBP1: A Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domain

• Published in: Archives of biochemistry and biophysics 2007-09, Vol.465 (2), p.399-409
• Main Authors: Lira, Cristina B.B., de Siqueira Neto, Jair L., Khater, Letícia, Cagliari, Thiago C., Peroni, Luis A., dos Reis, José R.R., Ramos, Carlos H.I., Cano, Maria I.N.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Binding Sites; DNA - chemistry; DNA-Binding Proteins - chemistry; Double-stranded DNA-binding protein; GT-rich DNA; Hydrophobic cavity; Leishmania - metabolism; Leishmania amazonensis; Molecular Sequence Data; Myb-like domain; Oncogene Proteins v-myb - chemistry; Protein Binding; Protein Structure, Tertiary; Telomere - chemistry; Telomeres
• ISSN: 0003-9861; 1096-0384
• DOI: 10.1016/j.abb.2007.06.020

Different species of Leishmania can cause a variety of medically important diseases, whose control and treatment are still health problems. Telomere binding proteins (TBPs) have potential as targets for anti-parasitic chemotherapy because of their importance for genome stability and cell viability. Here, we describe LaTBP1 a protein that has a Myb-like DNA-binding domain, a feature shared by most double-stranded telomeric proteins. Binding assays using full-length and truncated LaTBP1 combined with spectroscopy analysis were used to map the boundaries of the Myb-like domain near to the protein only tryptophan residue. The Myb-like domain of LaTBP1 contains a conserved hydrophobic cavity implicated in DNA-binding activity. A hypothetical model helped to visualize that it shares structural homology with domains of other Myb-containing proteins. Competition assays and chromatin immunoprecipitation confirmed the specificity of LaTBP1 for telomeric and GT-rich DNAs, suggesting that LaTBP1 is a new TBP.