9ULS

CryoEM structure of the T.thermophilus transcription initiation complex bound to Up4A-C and Up4A, -1 dA in the template DNA strand

これはPDB形式変換不可エントリーです。

9ULS の概要

• エントリーDOI: 10.2210/pdb9uls/pdb
• EMDBエントリー: 64266
• 分子名称: DNA-directed RNA polymerase subunit alpha, P1-(5'-Adenosyl) P4-(5'-uridyl) tetraphosphate, ZINC ION, ... (13 entities in total)
• 機能のキーワード: complex, transcription
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 461533.41

構造登録者

Duan, W.,Kaushik, A.,Serganov, A. (登録日: 2025-04-21, 公開日: 2025-10-22, 最終更新日: 2025-10-29)

主引用文献

Duan, W.,Kaushik, A.,Unarta, I.C.,Wu, Y.,Liu, M.M.J.,Weaver, J.W.,Wang, B.,Rice, W.J.,Luciano, D.J.,Belasco, J.G.,Huang, X.,Nudler, E.,Serganov, A.
Molecular basis for noncanonical transcription initiation from Np 4 A alarmones.
Nat.Chem.Biol., 2025

PubMed Abstract: Stress-induced dinucleoside tetraphosphates (NpNs, where N is adenosine, guanosine, cytosine or uridine) are ubiquitous in living organisms, yet their function has been largely elusive for over 50 years. Recent studies have revealed that RNA polymerase can influence the cellular lifetime of transcripts by incorporating these alarmones into RNA as 5'-terminal caps. Here we present structural and biochemical data that reveal the molecular basis of noncanonical transcription initiation from NpAs by Escherichia coli and Thermus thermophilus RNA polymerases. Our results show the influence of the first two nucleotide incorporation steps on capping efficiency and the different interactions of NpAs with transcription initiation complexes. These data provide critical insights into the substrate selectivity that dictates levels of Np capping in bacterial cells.

PubMed: 41094128
DOI: 10.1038/s41589-025-02044-6

実験手法

ELECTRON MICROSCOPY (2.5 Å)