8E95

Mycobacterium tuberculosis RNAP elongation complex

8E95 の概要

• エントリーDOI: 10.2210/pdb8e95/pdb
• EMDBエントリー: 27956
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total)
• 機能のキーワード: rna polymerase, transcription factor, elongation, pausing, transcription, transferase-dna-rna complex, transferase/dna/rna
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 403555.08

構造登録者

Delbeau, M.,Darst, S.A.,Campbell, E.A. (登録日: 2022-08-26, 公開日: 2023-03-22, 最終更新日: 2025-05-28)

主引用文献

Delbeau, M.,Omollo, E.O.,Froom, R.,Koh, S.,Mooney, R.A.,Lilic, M.,Brewer, J.J.,Rock, J.,Darst, S.A.,Campbell, E.A.,Landick, R.
Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosis.
Mol.Cell, 83:1474-1488.e8, 2023

PubMed Abstract: Transcriptional pauses mediate regulation of RNA biogenesis. DNA-encoded pause signals trigger pausing by stabilizing RNA polymerase (RNAP) swiveling and inhibiting DNA translocation. The N-terminal domain (NGN) of the only universal transcription factor, NusG/Spt5, modulates pausing through contacts to RNAP and DNA. Pro-pausing NusGs enhance pauses, whereas anti-pausing NusGs suppress pauses. Little is known about pausing and NusG in the human pathogen Mycobacterium tuberculosis (Mtb). We report that MtbNusG is pro-pausing. MtbNusG captures paused, swiveled RNAP by contacts to the RNAP protrusion and nontemplate-DNA wedged between the NGN and RNAP gate loop. In contrast, anti-pausing Escherichia coli (Eco) NGN contacts the MtbRNAP gate loop, inhibiting swiveling and pausing. Using CRISPR-mediated genetics, we show that pro-pausing NGN is required for mycobacterial fitness. Our results define an essential function of mycobacterial NusG and the structural basis of pro- versus anti-pausing NusG activity, with broad implications for the function of all NusG orthologs.

PubMed: 37116494
DOI: 10.1016/j.molcel.2023.04.007

実験手法

ELECTRON MICROSCOPY (2.9 Å)