Otro
LaTBP1: A Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domain
Registro en:
Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 465, n. 2, p. 399-409, 2007.
0003-9861
10.1016/j.abb.2007.06.020
WOS:000249570100011
Autor
Lira, Cristina B. B.
de Siqueira Neto, Jair L.
Khater, Leticia
Cagliari, Thiago C.
Peroni, Luis A.
dos Reis, Jose R. R.
Ramos, Carlos H. I.
Cano, Maria I. N.
Resumen
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. (C) 2007 Elsevier B.V. All rights reserved.