New sensor protein for phosphate dissociation during bacterial mRNA translation
Descripción del Articulo
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 Ini...
Autor: | |
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Formato: | tesis de grado |
Fecha de Publicación: | 2017 |
Institución: | Universidad Peruana de Ciencias Aplicadas |
Repositorio: | UPC-Institucional |
Lenguaje: | español |
OAI Identifier: | oai:repositorioacademico.upc.edu.pe:10757/621321 |
Enlace del recurso: | http://hdl.handle.net/10757/621321 |
Nivel de acceso: | acceso embargado |
Materia: | Biología molecular Proteínas Agentes antibacterianos Biosensores Hidrolisis Nutrición y Dietética |
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dc.title.es.fl_str_mv |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
title |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
spellingShingle |
New sensor protein for phosphate dissociation during bacterial mRNA translation Gencel Augusto, Jelica Biología molecular Proteínas Agentes antibacterianos Biosensores Hidrolisis Nutrición y Dietética |
title_short |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
title_full |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
title_fullStr |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
title_full_unstemmed |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
title_sort |
New sensor protein for phosphate dissociation during bacterial mRNA translation |
author |
Gencel Augusto, Jelica |
author_facet |
Gencel Augusto, Jelica |
author_role |
author |
dc.contributor.advisor.fl_str_mv |
Milon Mayer, Pohl Luis |
dc.contributor.author.fl_str_mv |
Gencel Augusto, Jelica |
dc.subject.es.fl_str_mv |
Biología molecular Proteínas Agentes antibacterianos Biosensores Hidrolisis Nutrición y Dietética |
topic |
Biología molecular Proteínas Agentes antibacterianos Biosensores Hidrolisis Nutrición y Dietética |
description |
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. |
publishDate |
2017 |
dc.date.accessioned.none.fl_str_mv |
2017-04-10T22:01:12Z |
dc.date.available.none.fl_str_mv |
2017-04-10T22:01:12Z |
dc.date.issued.fl_str_mv |
2017-03-01 |
dc.type.es.fl_str_mv |
info:eu-repo/semantics/bachelorThesis |
dc.type.other.es_PE.fl_str_mv |
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dc.identifier.citation.es_PE.fl_str_mv |
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 |
dc.identifier.uri.none.fl_str_mv |
http://hdl.handle.net/10757/621321 |
identifier_str_mv |
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 |
url |
http://hdl.handle.net/10757/621321 |
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Universidad Peruana de Ciencias Aplicadas (UPC) |
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PE |
dc.source.es_PE.fl_str_mv |
Universidad Peruana de Ciencias Aplicadas (UPC) Repositorio Académico - UPC |
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reponame:UPC-Institucional instname:Universidad Peruana de Ciencias Aplicadas instacron:UPC |
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4bac1de698405523bb83223998003265Milon Mayer, Pohl Luis6d09f87e195a898bc804fa2e8144a118500Gencel Augusto, Jelica2017-04-10T22:01:12Z2017-04-10T22:01:12Z2017-03-011. 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/10757/621321http://hdl.handle.net/10757/621321The 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.Tesisapplication/pdfapplication/epubapplication/mswordspaUniversidad Peruana de Ciencias Aplicadas (UPC)PEinfo:eu-repo/semantics/embargoedAccesshttp://purl.org/coar/access_right/c_f1cfUniversidad Peruana de Ciencias Aplicadas (UPC)Repositorio Académico - UPCreponame:UPC-Institucionalinstname:Universidad Peruana de Ciencias Aplicadasinstacron:UPCBiología molecularProteínasAgentes antibacterianosBiosensoresHidrolisisNutrición y DietéticaNew sensor protein for phosphate dissociation during bacterial mRNA translationinfo:eu-repo/semantics/bachelorThesisTesishttp://purl.org/coar/resource_type/c_7a1fSUNEDUUniversidad Peruana de Ciencias Aplicadas (UPC). Facultad de Ciencias de la SaludLicenciaturaNutrición y DietéticaLicenciado en Nutrición y Dietética2018-03-01T00:00:00ZThe 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. 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