Cloning And Characterization Of Three Hypothetical Secretion Chaperone Proteins From Xanthomonas Axonopodis Pv. Citri.

dc.creatorTasic, Ljubica
dc.creatorBorin, Paula F L
dc.creatorKhater, Leti Cia
dc.creatorRamos, Carlos H I
dc.date2007-Jun
dc.date2015-11-27T13:09:52Z
dc.date2015-11-27T13:09:52Z
dc.date.accessioned2018-03-29T01:04:27Z
dc.date.available2018-03-29T01:04:27Z
dc.identifierProtein Expression And Purification. v. 53, n. 2, p. 363-9, 2007-Jun.
dc.identifier1046-5928
dc.identifier10.1016/j.pep.2007.01.011
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/17350859
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/197198
dc.identifier17350859
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1297431
dc.descriptionXanthomonas axonopodis pv. citri (Xac) causes citrus canker in plantations around the world and is of particular significance in Brazil where its incidence has risen exponentially over the past decade. Approximately one third of the predicted Xac open reading frames show no homology, or homology with very low score with that of known sequences. It is believed that Xac utilizes secretion systems to transfer virulence proteins into susceptible eukaryotic cells. This process is assisted by secretion chaperones that maintain virulence proteins partly or completely unfolded during translocation. We have cloned three of these hypothetical secretion chaperones: XAC0419 and XAC1346 from type III secretion system (TTSS) and XACb0033 from type IV secretion system (TFSS). All proteins were cloned in a pET23a vector (Novagen), expressed at 37 degrees C using a BL21(DE3)pLysS Escherichia coli strain and purified by ion exchange and gel-filtration chromatographic methods. Pure proteins were characterized using spectroscopic measurements: circular dichroism, and both static and lifetime emission fluorescence in the case of XACb0033. The analyzed proteins are stable at elevated temperatures (up to 65 degrees C) and exhibit alpha-helix content from approximately 30% (XACb003) to approximately 87% (XAC1346). XACb0033 exhibits lifetimes in the fluorescence experiments that indicate different neighborhoods for its tryptophan residues. These chaperones have the characteristics of TTSS and TFSS: all are small, with a high alpha-helix content, and without ATP-binding or ATP-hydrolyzing activity.
dc.description53
dc.description363-9
dc.languageeng
dc.relationProtein Expression And Purification
dc.relationProtein Expr. Purif.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectBacterial Proteins
dc.subjectCircular Dichroism
dc.subjectCitrus
dc.subjectCloning, Molecular
dc.subjectEscherichia Coli
dc.subjectGene Expression
dc.subjectGenes, Bacterial
dc.subjectMolecular Chaperones
dc.subjectMolecular Sequence Data
dc.subjectNuclear Magnetic Resonance, Biomolecular
dc.subjectPlant Diseases
dc.subjectProtein Structure, Secondary
dc.subjectRecombinant Proteins
dc.subjectSpectrometry, Fluorescence
dc.subjectVirulence
dc.subjectXanthomonas Axonopodis
dc.titleCloning And Characterization Of Three Hypothetical Secretion Chaperone Proteins From Xanthomonas Axonopodis Pv. Citri.
dc.typeArtículos de revistas


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