Electronic Resource
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
| العنوان: | 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 |
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| المؤلفون: | Fernández-Tornero, Carlos, Ministerio de Economía, Industria y Competitividad (España), Alegrio Louro, Jaime |
| بيانات النشر: | CSIC - Centro de Investigaciones Biológicas Margarita Salas (CIB) Universidad Autónoma de Madrid 2017 |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | 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. |
| مصطلحات الفهرس: | Growth control, Ribosomal RNA, Ribosomal DNA, Transcription, RNA polymerase I, Cryo-EM, CryoEM, Macromolecular complex, tesis doctoral |
| URL: | Sí |
| الاتاحة: | Open access content. Open access content openAccess |
| ملاحظة: | Spanish |
| Other Numbers: | CTK oai:digital.csic.es:10261/156259 1105211756 |
| المصدر المساهم: | CSIC From OAIster®, provided by the OCLC Cooperative. |
| رقم الانضمام: | edsoai.on1105211756 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |