7ASV
Crystal structure of tWHD2 of Rpc5 subunit of human RNA Polymerase III
7ASV の概要
エントリーDOI | 10.2210/pdb7asv/pdb |
分子名称 | DNA-directed RNA polymerase III subunit RPC5, ACETATE ION (3 entities in total) |
機能のキーワード | rna pol iii, rna polymerase iii, transcription, rpc5 |
由来する生物種 | Homo sapiens (Human) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 162268.12 |
構造登録者 | |
主引用文献 | Ramsay, E.P.,Abascal-Palacios, G.,Daiss, J.L.,King, H.,Gouge, J.,Pilsl, M.,Beuron, F.,Morris, E.,Gunkel, P.,Engel, C.,Vannini, A. Structure of human RNA polymerase III. Nat Commun, 11:6409-6409, 2020 Cited by PubMed Abstract: In eukaryotes, RNA Polymerase (Pol) III is specialized for the transcription of tRNAs and other short, untranslated RNAs. Pol III is a determinant of cellular growth and lifespan across eukaryotes. Upregulation of Pol III transcription is observed in cancer and causative Pol III mutations have been described in neurodevelopmental disorders and hypersensitivity to viral infection. Here, we report a cryo-EM reconstruction at 4.0 Å of human Pol III, allowing mapping and rationalization of reported genetic mutations. Mutations causing neurodevelopmental defects cluster in hotspots affecting Pol III stability and/or biogenesis, whereas mutations affecting viral sensing are located in proximity to DNA binding regions, suggesting an impairment of Pol III cytosolic viral DNA-sensing. Integrating x-ray crystallography and SAXS, we also describe the structure of the higher eukaryote specific RPC5 C-terminal extension. Surprisingly, experiments in living cells highlight a role for this module in the assembly and stability of human Pol III. PubMed: 33335104DOI: 10.1038/s41467-020-20262-5 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.55 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
