Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state

127 p.-18 fig.-17 tab.

Detalhes bibliográficos
Autor: Alegrio Louro, Jaime
Formato: tesis doctoral
Fecha de publicación:2017
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/156259
Acesso em linha:http://hdl.handle.net/10261/156259
Access Level:acceso abierto
Palavra-chave:Growth control
Ribosomal RNA
Ribosomal DNA
Transcription
RNA polymerase I
Cryo-EM
CryoEM
Macromolecular complex
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spelling Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated stateAlegrio Louro, JaimeGrowth controlRibosomal RNARibosomal DNATranscriptionRNA polymerase ICryo-EMCryoEMMacromolecular complex127 p.-18 fig.-17 tab.In eukaryotes, DNA polymerase I is the kilodalton enzyme responsible for ribosonal DNA (rDNA) transcription, leading to the synthesis of the ribosonal RNA precusor. Pol I's activity is crucial for ribosome biogenesis and therefore, its modulation influences cell growth. The intiation factor rDNA, conseved in eukaryotes, binds Pol I corresponds to an activated state of the enzyme, whose activity can be regulated by assembling or disrupting Pol I:Rm3. the cryo-electron microscopy (cryo-EM) structures of yeast free monomeric Pol I at 4.9 A resolution and Pol I in complex with Rm3 at 7.7 A are the major findings reported here. The derived pseudo-atomic models unveil the structural changes in the transition from inactive Pol I dimers. previously solved by X-ray crystalography, to free monovers and from these to the activated state bound to Rm.3 In addition, analytical ultracentrifugation suggets that yeast Rm3 dimers found in solution migth establish a dimer-monover equilibrium in vitro upon dilution. Also, electrophoretic mobility shift assays indicate yeast Rm3 could not bind DNA as previously described for the mammalian homolog. These resuts provide valuable information on Pol I and Rn3 changes required for enzyme activation.Beca FPI BES-2011-044359 del Ministerio de Economía Industria y CompetitividadPeer reviewedCSIC - Centro de Investigaciones Biológicas Margarita Salas (CIB)Universidad Autónoma de MadridFernández-Tornero, CarlosMinisterio de Economía, Industria y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201720172017info:eu-repo/semantics/doctoralThesishttp://purl.org/coar/resource_type/c_db06http://hdl.handle.net/10261/156259reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)EspañolSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1562592026-05-22T06:33:51Z
dc.title.none.fl_str_mv Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
title Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
spellingShingle Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
Alegrio Louro, Jaime
Growth control
Ribosomal RNA
Ribosomal DNA
Transcription
RNA polymerase I
Cryo-EM
CryoEM
Macromolecular complex
title_short Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
title_full Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
title_fullStr Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
title_full_unstemmed Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
title_sort Cryo-em structures of free monomeric and RRN3-bound RNA polynerase I unveil the structural changes in the transition fom inactive dimers to the activated state
dc.creator.none.fl_str_mv Alegrio Louro, Jaime
author Alegrio Louro, Jaime
author_facet Alegrio Louro, Jaime
author_role author
dc.contributor.none.fl_str_mv Fernández-Tornero, Carlos
Ministerio de Economía, Industria y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Growth control
Ribosomal RNA
Ribosomal DNA
Transcription
RNA polymerase I
Cryo-EM
CryoEM
Macromolecular complex
topic Growth control
Ribosomal RNA
Ribosomal DNA
Transcription
RNA polymerase I
Cryo-EM
CryoEM
Macromolecular complex
description 127 p.-18 fig.-17 tab.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/doctoralThesis
http://purl.org/coar/resource_type/c_db06
format doctoralThesis
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/156259
url http://hdl.handle.net/10261/156259
dc.language.none.fl_str_mv Español
language_invalid_str_mv Español
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv CSIC - Centro de Investigaciones Biológicas Margarita Salas (CIB)
Universidad Autónoma de Madrid
publisher.none.fl_str_mv CSIC - Centro de Investigaciones Biológicas Margarita Salas (CIB)
Universidad Autónoma de Madrid
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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