LaTBP1: a Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domain.
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.
Departamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Botucatu 18618-000, SP, Brazil.
Cristina B B
CB
Lira
Jair L
JL
de Siqueira Neto
Letícia
L
Khater
Thiago C
TC
Cagliari
Luis A
LA
Peroni
José R R
JR
dos Reis
Carlos H I
CH
Ramos
Maria I N
MI
Cano
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D007891:Leishmania / Q000378:metabolism*; D008969:Molecular Sequence Data; D020626:Oncogene Proteins v-myb / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016615:Telomere / Q000737:chemistry*
D004268:DNA-Binding Proteins; D020626:Oncogene Proteins v-myb; D004247:DNA