7D58
cryo-EM structure of human RNA polymerase III in elongating state
7D58 の概要
| エントリーDOI | 10.2210/pdb7d58/pdb |
| EMDBエントリー | 30577 |
| 分子名称 | 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, ... (22 entities in total) |
| 機能のキーワード | rna polymerase iii, transcription |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 20 |
| 化学式量合計 | 740737.12 |
| 構造登録者 | |
| 主引用文献 | Wang, Q.,Li, S.,Wan, F.,Xu, Y.,Wu, Z.,Cao, M.,Lan, P.,Lei, M.,Wu, J. Structural insights into transcriptional regulation of human RNA polymerase III. Nat.Struct.Mol.Biol., 28:220-227, 2021 Cited by PubMed Abstract: RNA polymerase III (Pol III) synthesizes structured, essential small RNAs, such as transfer RNA, 5S ribosomal RNA and U6 small nuclear RNA. Pol III, the largest nuclear RNA polymerase, is composed of a conserved core region and eight constitutive regulatory subunits, but how these factors jointly regulate Pol III transcription remains unclear. Here, we present cryo-EM structures of human Pol III in both apo and elongating states, which unveil both an orchestrated movement during the apo-to-elongating transition and an unexpected apo state in which the RPC7 subunit tail occupies the DNA-RNA-binding cleft of Pol III, suggesting that RPC7 plays important roles in both autoinhibition and transcription initiation. The structures also reveal a proofreading mechanism for the TFIIS-like subunit RPC10, which stably retains its catalytic position in the secondary channel, explaining the high fidelity of Pol III transcription. Our work provides an integrated picture of the mechanism of Pol III transcription regulation. PubMed: 33558766DOI: 10.1038/s41594-021-00557-x 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.9 Å) |
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