2K06

Solution structure of the aminoterminal domain of E. coli NusG

2K06 の概要

• エントリーDOI: 10.2210/pdb2k06/pdb
• NMR情報: BMRB: 15642
• 分子名称: Transcription antitermination protein nusG (1 entity in total)
• 機能のキーワード: nusg, transcription, transcription antitermination, transcription regulation, transcription termination
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14096.26

構造登録者

Schweimer, K.,Scheckenhofer, U.,Roesch, P. (登録日: 2008-01-25, 公開日: 2009-02-03, 最終更新日: 2024-05-01)

主引用文献

Mooney, R.A.,Schweimer, K.,Rosch, P.,Gottesman, M.,Landick, R.
Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators.
J.Mol.Biol., 391:341-358, 2009

PubMed Abstract: NusG is a conserved regulatory protein that interacts with elongation complexes (ECs) of RNA polymerase, DNA, and RNA to modulate transcription in multiple and sometimes opposite ways. In Escherichia coli, NusG suppresses pausing and increases elongation rate, enhances termination by E. coli rho and phage HK022 Nun protein, and promotes antitermination by lambdaN and in ribosomal RNA operons. We report NMR studies that suggest that E. coli NusG consists of two largely independent N- and C-terminal structural domains, NTD and CTD, respectively. Based on tests of the functions of the NTD and CTD and variants of NusG in vivo and in vitro, we find that NTD alone is sufficient to suppress pausing and enhance transcript elongation in vitro. However, neither domain alone can enhance rho-dependent termination or support antitermination, indicating that interactions of both domains with ECs are required for these processes. We propose that the two domains of NusG mediate distinct interactions with ECs: the NTD interacts with RNA polymerase and the CTD interacts with rho and other regulators, providing NusG with different combinations of interactions to effect different regulatory outcomes.

PubMed: 19500594
DOI: 10.1016/j.jmb.2009.05.078

実験手法

SOLUTION NMR