7Z30

Structure of yeast RNA Polymerase III-Ty1 integrase complex at 2.9 A (focus subunit C11 terminal Zn-ribbon in the funnel pore).

これはPDB形式変換不可エントリーです。

7Z30 の概要

• エントリーDOI: 10.2210/pdb7z30/pdb
• EMDBエントリー: 14469
• 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: targeted dna integration, ty1 retrotransposon, ty1 integrase, rna 19 polymerase iii, transcription
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 19
• 化学式量合計: 762630.80

構造登録者

Nguyen, P.Q.,Fernandez-Tornero, C. (登録日: 2022-03-01, 公開日: 2023-04-05, 最終更新日: 2024-07-17)

主引用文献

Nguyen, P.Q.,Huecas, S.,Asif-Laidin, A.,Plaza-Pegueroles, A.,Capuzzi, B.,Palmic, N.,Conesa, C.,Acker, J.,Reguera, J.,Lesage, P.,Fernandez-Tornero, C.
Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.
Nat Commun, 14:1729-1729, 2023

PubMed Abstract: The yeast Ty1 retrotransposon integrates upstream of genes transcribed by RNA polymerase III (Pol III). Specificity of integration is mediated by an interaction between the Ty1 integrase (IN1) and Pol III, currently uncharacterized at the atomic level. We report cryo-EM structures of Pol III in complex with IN1, revealing a 16-residue segment at the IN1 C-terminus that contacts Pol III subunits AC40 and AC19, an interaction that we validate by in vivo mutational analysis. Binding to IN1 associates with allosteric changes in Pol III that may affect its transcriptional activity. The C-terminal domain of subunit C11, involved in RNA cleavage, inserts into the Pol III funnel pore, providing evidence for a two-metal mechanism during RNA cleavage. Additionally, ordering next to C11 of an N-terminal portion from subunit C53 may explain the connection between these subunits during termination and reinitiation. Deletion of the C53 N-terminal region leads to reduced chromatin association of Pol III and IN1, and a major fall in Ty1 integration events. Our data support a model in which IN1 binding induces a Pol III configuration that may favor its retention on chromatin, thereby improving the likelihood of Ty1 integration.

PubMed: 36977686
DOI: 10.1038/s41467-023-37109-4

実験手法

ELECTRON MICROSCOPY (2.9 Å)