EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Allosteric mechanism of transcription inhibition by NusG-dependent pausing of RNA polymerase.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 120, Issue 7, Page e2218516120, Year 2023
掲載日	2023年2月14日
著者	Rishi K Vishwakarma / M Zuhaib Qayyum / Paul Babitzke / Katsuhiko S Murakami /
PubMed 要旨	NusG is a transcription elongation factor that stimulates transcription pausing in Gram+ bacteria including by sequence-specific interaction with a conserved pause-inducing TTNTTT motif found in the ...NusG is a transcription elongation factor that stimulates transcription pausing in Gram+ bacteria including by sequence-specific interaction with a conserved pause-inducing TTNTTT motif found in the non-template DNA (ntDNA) strand within the transcription bubble. To reveal the structural basis of NusG-dependent pausing, we determined a cryo-EM structure of a paused transcription complex (PTC) containing RNA polymerase (RNAP), NusG, and the TTNTTT motif in the ntDNA strand. The interaction of NusG with the ntDNA strand rearranges the transcription bubble by positioning three consecutive T residues in a cleft between NusG and the β-lobe domain of RNAP. We revealed that the RNAP swivel module rotation (swiveling), which widens (swiveled state) and narrows (non-swiveled state) a cleft between NusG and the β-lobe, is an intrinsic motion of RNAP and is directly linked to trigger loop (TL) folding, an essential conformational change of all cellular RNAPs for the RNA synthesis reaction. We also determined cryo-EM structures of RNAP escaping from the paused transcription state. These structures revealed the NusG-dependent pausing mechanism by which NusG-ntDNA interaction inhibits the transition from swiveled to non-swiveled states, thereby preventing TL folding and RNA synthesis allosterically. This motion is also reduced by the formation of an RNA hairpin within the RNA exit channel. Thus, the pause half-life can be modulated by the strength of the NusG-ntDNA interaction and/or the stability of the RNA hairpin. NusG residues that interact with the TTNTTT motif are widely conserved in bacteria, suggesting that NusG-dependent pausing is widespread.
リンク	Proc Natl Acad Sci U S A / PubMed:36745813 / PubMed Central
手法	EM (単粒子)
解像度	3.0 - 3.3 Å
構造データ	28149 8ehq EMDB-28149, PDB-8ehq: Mycobacterium tuberculosis paused transcription complex with Bacillus subtilis NusG 手法: EM (単粒子) / 解像度: 3.0 Å 28174 8ej3 EMDB-28174, PDB-8ej3: M. tuberculosis RNAP pause escaped complex with Bacillus subtilis NusG and GMPCPP 手法: EM (単粒子) / 解像度: 3.13 Å 28373 8eoe EMDB-28373, PDB-8eoe: Mycobacterium tuberculosis transcription elongation complex with Bacillus subtilis NusG (EC_LG) 手法: EM (単粒子) / 解像度: 3.2 Å 28374 8eof EMDB-28374, PDB-8eof: Mycobacterium tuberculosis transcription elongation complex with Bacillus subtilis NusG (EC_PG) 手法: EM (単粒子) / 解像度: 3.3 Å 28466 8eos EMDB-28466, PDB-8eos: M. tuberculosis RNAP elongation complex with NusG and CMPCPP 手法: EM (単粒子) / 解像度: 3.1 Å 28467 8eot EMDB-28467, PDB-8eot: M. tuberculosis RNAP elongation complex with NusG 手法: EM (単粒子) / 解像度: 3.3 Å 28665 8exy EMDB-28665, PDB-8exy: M. tuberculosis RNAP paused complex with B. subtilis NusG and GMPCPP 手法: EM (単粒子) / 解像度: 3.2 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ZN: Unknown entry ChemComp-G2P: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMPCPP / GMP-CPP, エネルギー貯蔵分子類似体YM ChemComp-2TM*: 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]cytidine / 5′-シチジルオキシホスホニルメチルホスホニルオキシホスホン酸
由来	mycobacterium tuberculosis h37rv (結核菌) bacillus subtilis subsp. subtilis str. 168 (枯草菌) synthetic construct (人工物) synthetic rna (人工物)
キーワード	TRANSCRIPTION (転写 (生物学)) / Transcription elongation RNA polymerase pausing NusG cryo-EM / RNA polymerase pausing NusG cryo-EM