5LMX
Monomeric RNA polymerase I at 4.9 A resolution
Summary for 5LMX
Entry DOI | 10.2210/pdb5lmx/pdb |
EMDB information | 4088 |
Descriptor | DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (15 entities in total) |
Functional Keywords | multi-protein complex, rna polymerase, monomeric form, transcription |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 14 |
Total formula weight | 595788.78 |
Authors | Torreira, E.,Louro, J.A.,Gil-Carton, D.,Gallego, O.,Calvo, O.,Fernandez-Tornero, C. (deposition date: 2016-08-02, release date: 2017-03-22, Last modification date: 2024-05-15) |
Primary citation | Torreira, E.,Louro, J.A.,Pazos, I.,Gonzalez-Polo, N.,Gil-Carton, D.,Duran, A.G.,Tosi, S.,Gallego, O.,Calvo, O.,Fernandez-Tornero, C. The dynamic assembly of distinct RNA polymerase I complexes modulates rDNA transcription. Elife, 6:-, 2017 Cited by PubMed Abstract: Cell growth requires synthesis of ribosomal RNA by RNA polymerase I (Pol I). Binding of initiation factor Rrn3 activates Pol I, fostering recruitment to ribosomal DNA promoters. This fundamental process must be precisely regulated to satisfy cell needs at any time. We present in vivo evidence that, when growth is arrested by nutrient deprivation, cells induce rapid clearance of Pol I-Rrn3 complexes, followed by the assembly of inactive Pol I homodimers. This dual repressive mechanism reverts upon nutrient addition, thus restoring cell growth. Moreover, Pol I dimers also form after inhibition of either ribosome biogenesis or protein synthesis. Our mutational analysis, based on the electron cryomicroscopy structures of monomeric Pol I alone and in complex with Rrn3, underscores the central role of subunits A43 and A14 in the regulation of differential Pol I complexes assembly and subsequent promoter association. PubMed: 28262097DOI: 10.7554/eLife.20832 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.9 Å) |
Structure validation
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