dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Estadual de Campinas (UNICAMP)
dc.contributorLab Nacl Luz Sincrot
dc.date.accessioned2014-05-20T13:50:06Z
dc.date.available2014-05-20T13:50:06Z
dc.date.created2014-05-20T13:50:06Z
dc.date.issued2007-09-15
dc.identifierArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 465, n. 2, p. 399-409, 2007.
dc.identifier0003-9861
dc.identifierhttp://hdl.handle.net/11449/17878
dc.identifier10.1016/j.abb.2007.06.020
dc.identifierWOS:000249570100011
dc.description.abstractDifferent 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.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationArchives of Biochemistry and Biophysics
dc.relation3.118
dc.relation1,350
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectdouble-stranded DNA-binding protein
dc.subjectGT-rich DNA
dc.subjecthydrophobic cavity
dc.subjectleishmania amazonensis
dc.subjectmyb-like domain
dc.subjecttelomeres
dc.titleLaTBP1: A Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domain
dc.typeArtículos de revistas


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