Repository logo

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

Loading...
Thumbnail Image

Advisor

Coadvisor

Graduate program

Undergraduate course

Journal Title

Journal ISSN

Volume Title

Publisher

Elsevier B.V.
Elsevier

Type

Article

Access right

Acesso restrito

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. (C) 2007 Elsevier B.V. All rights reserved.

Description

Language

English

Citation

Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 465, n. 2, p. 399-409, 2007.

Related itens

Sponsors

Units

Item type:Unit,
Botucatu, Instituto de Biociências - IBB
IBB
Campus: Botucatu

Departments

Undergraduate courses

Graduate programs