Summary for 7Z1O
| Entry DOI | 10.2210/pdb7z1o/pdb |
| Related | 7Z1L 7Z1M 7Z1N |
| EMDB information | 14451 |
| Descriptor | DNA-directed RNA polymerase III subunit RPC1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (23 entities in total) |
| Functional Keywords | rna synthesis, short rnas, termination, transcription |
| Biological source | Saccharomyces cerevisiae W303 More |
| Total number of polymer chains | 20 |
| Total formula weight | 729597.61 |
| Authors | Girbig, M.,Mueller, C.W. (deposition date: 2022-02-24, release date: 2022-08-31, Last modification date: 2024-07-17) |
| Primary citation | Girbig, M.,Xie, J.,Grotsch, H.,Libri, D.,Porrua, O.,Muller, C.W. Architecture of the yeast Pol III pre-termination complex and pausing mechanism on poly(dT) termination signals. Cell Rep, 40:111316-111316, 2022 Cited by PubMed Abstract: RNA polymerase (Pol) III is specialized to transcribe short, abundant RNAs, for which it terminates transcription on polythymine (dT) stretches on the non-template (NT) strand. When Pol III reaches the termination signal, it pauses and forms the pre-termination complex (PTC). Here, we report cryoelectron microscopy (cryo-EM) structures of the yeast Pol III PTC and complementary functional states at resolutions of 2.7-3.9 Å. Pol III recognizes the poly(dT) termination signal with subunit C128 that forms a hydrogen-bond network with the NT strand and, thereby, induces pausing. Mutating key interacting residues interferes with transcription termination in vitro, impairs yeast growth, and causes global termination defects in vivo, confirming our structural results. Additional cryo-EM analysis reveals that C53-C37, a Pol III subcomplex and key termination factor, participates indirectly in Pol III termination. We propose a mechanistic model of Pol III transcription termination and rationalize why Pol III, unlike Pol I and Pol II, terminates on poly(dT) signals. PubMed: 36070694DOI: 10.1016/j.celrep.2022.111316 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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