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dc.contributor.authorManzine, Livia Regina
dc.contributor.authorAlves da Silva, Marco Tulio
dc.contributor.authorThiemann, Otavio Henrique
dc.contributor.authorCicarelli, Regina Maria Barretto [UNESP]
dc.date.accessioned2014-05-20T13:24:34Z
dc.date.available2014-05-20T13:24:34Z
dc.date.issued2006-11-01
dc.identifierhttp://www.rcin.org.pl/dlibra/docmetadata?id=13542&from=publication
dc.identifier.citationActa Protozoologica. Warsaw: Nencki Inst Experimental Biology, v. 45, n. 4, p. 367-375, 2006.
dc.identifier.issn0065-1583
dc.identifier.urihttp://hdl.handle.net/11449/7655
dc.description.abstractBlastocrithidia culicis is a protozoan of the family Trypanosomatidae. It is a parasite of insects, but the presence of bacteriumlike endosymbionts in its cytoplasm led some investigators to study this protozoan. This trypanosomatid does not infect humans and although it is phylogenetically distant from Trypanosoma cruzi, it presents many morphological characteristics, which are similar. In previous studies our group showed the presence of a L27 ribosomal protein in T cruzi (named TcrL27) using a RT-PCR, which also resulted in the cloning, sequencing and expression of an unexpected ribosomal protein, L17, in Blastocrithidia culicis (BcL17). In this paper, Western blot analysis demonstrated that the anti-BcL17 antibody recognizes the presence of the same ribosomal protein either in Blastochritidia culicis and T. cruzi nuclear extracts. Besides, two similar bands (40 and 47 kDa) appeared also in T. cruzi isolated ribosomal proteins and B. culicis nuclear extract corroborating with the findings showed in the phylogenetic reconstruction. With respect to their localization within the ribosome, both the L17 and L27 ribosomal proteins appear to belong to the peptidyl-transferase site, and are therefore part of the key step in protein synthesis. Both ribosomal proteins bind spiramycin derivatives, being therefore compounds of the macrolides connection sites in the ribosome. These findings would open a possibility to better evaluate this issue.en
dc.format.extent367-375
dc.language.isoeng
dc.publisherNencki Inst Experimental Biology
dc.relation.ispartofActa Protozoologica
dc.sourceWeb of Science
dc.subjectBlastocrithidia culicispt
dc.subjectL17 ribosomal proteinpt
dc.subjectrecombinant ribosomal proteinpt
dc.subjecttrypanosomatidspt
dc.titleMolecular characterization of Blastocrithidia culicis L17 ribosomal proteinen
dc.typeArtigo
dcterms.licensehttp://www.eko.uj.edu.pl/ap/index.php?option=com_content&task=view&id=23&Itemid=50
dcterms.rightsHolderNencki Inst Experimental Biology
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUniv Estadual Paulista, Dept Ciências Biol, Fac Ciências Farmaceut, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Fis Sao Carlos, Sao Carlos, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Dept Ciências Biol, Fac Ciências Farmaceut, BR-14801902 Araraquara, SP, Brazil
dc.identifier.wosWOS:000243318800004
dc.rights.accessRightsAcesso aberto
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
dc.identifier.fileWOS000243318800004.pdf
dc.relation.ispartofjcr1.038
dc.relation.ispartofsjr0,466
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