New sensor protein for phosphate dissociation during bacterial mRNA translation

2.50
Hdl Handle:
http://hdl.handle.net/10757/621321
Title:
New sensor protein for phosphate dissociation during bacterial mRNA translation
Authors:
Gencel Augusto, Jelica
Advisors:
Milón Mayer, Pohl Luis
Citation:
1. Augusto G. New sensor protein for phosphate dissociation during bacterial mRNA translation Acknowledgments [Internet]. Universidad Peruana de Ciencias Aplicadas (UPC); 2017. Available from: http://hdl.handle.net/10757/621321
Publisher:
Universidad Peruana de Ciencias Aplicadas (UPC)
Issue Date:
1
URI:
http://hdl.handle.net/10757/621321
Abstract:
The translation initiation process is an important checkpoint that assures the correct protein production. Within this phase, Initiation Factor IF2 plays an important role along all early and late steps of the process. During late reactions, IF2 enhances the joining of the 50S subunit to the 30S Initiation Complex (IC) and positions initiator tRNA in the 70S IC. Concomitantly, IF2 hydrolyses a GTP molecule which led to propose that the active hydrolysis of GTP stimulates both above events. However, recent mutagenic studies of IF2 showed that inhibiting its GTP hydrolytic activity does not compromise the overall translation initiation process. Moreover, biochemical studies indicate that the dissociation of inorganic phosphate (Pi) is a late event, prior to the release of IF2. These findings indicated that it is the dissociation of Pi that weakens the interaction of IF2 with the ribosome. However, the GTP hydrolysis reaction is energetically favorable and may actively drive factor release. To elucidate which of the above postulates describe more accurately IF2 dependent reactions, here we design, produce and test a novel recombinant fluorescent phosphate binding sensor that specifically binds nearby the exit point of Pi during protein translation. This protein chimeras could evidence whether the IF2 dissociation is catalyzed by the Pi dissociation after GTP hydrolysis or by the reaction per se. Furthermore, the system provides a novel platform to study and systematically screen for new antimicrobial compounds.
Type:
info:eu-repo/semantics/bachelorThesis
Rights:
info:eu-repo/semantics/embargoedAccess
Language:
spa
Keywords:
Biología molecular; Proteínas; Agentes antibacterianos; Biosensores; Hidrolisis; Nutrición y Dietética

Full metadata record

DC FieldValue Language
dc.contributor.advisorMilón Mayer, Pohl Luises
dc.contributor.authorGencel Augusto, Jelicaes
dc.date.accessioned2017-04-10T22:01:12Z-
dc.date.available2017-04-10T22:01:12Z-
dc.date.issued01/03/2017-
dc.identifier.citation1. Augusto G. New sensor protein for phosphate dissociation during bacterial mRNA translation Acknowledgments [Internet]. Universidad Peruana de Ciencias Aplicadas (UPC); 2017. Available from: http://hdl.handle.net/10757/621321es_PE
dc.identifier.urihttp://hdl.handle.net/10757/621321-
dc.description.abstractThe translation initiation process is an important checkpoint that assures the correct protein production. Within this phase, Initiation Factor IF2 plays an important role along all early and late steps of the process. During late reactions, IF2 enhances the joining of the 50S subunit to the 30S Initiation Complex (IC) and positions initiator tRNA in the 70S IC. Concomitantly, IF2 hydrolyses a GTP molecule which led to propose that the active hydrolysis of GTP stimulates both above events. However, recent mutagenic studies of IF2 showed that inhibiting its GTP hydrolytic activity does not compromise the overall translation initiation process. Moreover, biochemical studies indicate that the dissociation of inorganic phosphate (Pi) is a late event, prior to the release of IF2. These findings indicated that it is the dissociation of Pi that weakens the interaction of IF2 with the ribosome. However, the GTP hydrolysis reaction is energetically favorable and may actively drive factor release. To elucidate which of the above postulates describe more accurately IF2 dependent reactions, here we design, produce and test a novel recombinant fluorescent phosphate binding sensor that specifically binds nearby the exit point of Pi during protein translation. This protein chimeras could evidence whether the IF2 dissociation is catalyzed by the Pi dissociation after GTP hydrolysis or by the reaction per se. Furthermore, the system provides a novel platform to study and systematically screen for new antimicrobial compounds.es
dc.description.uriTesises_PE
dc.formatapplication/pdfes
dc.formatapplication/epubes
dc.formatapplication/mswordes
dc.language.isospaes
dc.publisherUniversidad Peruana de Ciencias Aplicadas (UPC)es
dc.rightsinfo:eu-repo/semantics/embargoedAccesses
dc.sourceUniversidad Peruana de Ciencias Aplicadas (UPC)es_PE
dc.sourceRepositorio Académico - UPCes_PE
dc.subjectBiología moleculares
dc.subjectProteínases
dc.subjectAgentes antibacterianoses
dc.subjectBiosensoreses
dc.subjectHidrolisises
dc.subjectNutrición y Dietéticaes
dc.titleNew sensor protein for phosphate dissociation during bacterial mRNA translationes
dc.typeinfo:eu-repo/semantics/bachelorThesises
thesis.degree.grantorUniversidad Peruana de Ciencias Aplicadas (UPC). Facultad de Ciencias de la Saludes_PE
thesis.degree.levelLicenciaturaes_PE
thesis.degree.disciplineNutrición y Dietéticaes_PE
thesis.degree.nameLicenciado en Nutrición y Dietéticaes_PE
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