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

Abstract

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.

• Authors: Cristina B B Lira, Jair L de Siqueira Neto, Letícia Khater, Thiago C Cagliari, Luis A Peroni, José R R dos Reis, Carlos H I Ramos, Maria I N Cano
• Journal: Archives of biochemistry and biophysics (Arch Biochem Biophys) Vol. 465 Issue 2 Pg. 399-409 (Sep 15 2007) ISSN: 0003-9861 [Print] United States
• PMID: 17678615 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• DNA-Binding Proteins
• Oncogene Proteins v-myb
• DNA

Topics

• Amino Acid Sequence
• Animals
• Binding Sites
• DNA (chemistry)
• DNA-Binding Proteins (chemistry)
• Leishmania (metabolism)
• Molecular Sequence Data
• Oncogene Proteins v-myb (chemistry)
• Protein Binding
• Protein Structure, Tertiary
• Telomere (chemistry)