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

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dc.contributor.authorLira, Cristina B. B.
dc.contributor.authorde Siqueira Neto, Jair L.
dc.contributor.authorKhater, Leticia
dc.contributor.authorCagliari, Thiago C.
dc.contributor.authorPeroni, Luis A.
dc.contributor.authordos Reis, Jose R. R.
dc.contributor.authorRamos, Carlos H. I.
dc.contributor.authorCano, Maria I. N.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionLab Nacl Luz Sincrot
dc.date.accessioned2014-05-20T13:50:06Z
dc.date.available2014-05-20T13:50:06Z
dc.date.issued2007-09-15
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.en
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias, Dept Genet, Botucatu, SP, Brazil
dc.description.affiliationUniv Estadual Campinas, Inst Biol, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationLab Nacl Luz Sincrot, Campinas, SP, Brazil
dc.description.affiliationUniv Estadual Campinas, Inst Quim, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias, Dept Genet, Botucatu, SP, Brazil
dc.format.extent399-409
dc.identifierhttp://dx.doi.org/10.1016/j.abb.2007.06.020
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 465, n. 2, p. 399-409, 2007.
dc.identifier.doi10.1016/j.abb.2007.06.020
dc.identifier.issn0003-9861
dc.identifier.urihttp://hdl.handle.net/11449/17878
dc.identifier.wosWOS:000249570100011
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.relation.ispartofjcr3.118
dc.relation.ispartofsjr1,350
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectdouble-stranded DNA-binding proteinpt
dc.subjectGT-rich DNApt
dc.subjecthydrophobic cavitypt
dc.subjectleishmania amazonensispt
dc.subjectmyb-like domainpt
dc.subjecttelomerespt
dc.titleLaTBP1: A Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domainen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.orcid0000-0002-7246-9081[7]
unesp.author.orcid0000-0001-9574-8174[2]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt

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