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	In transcription antitermination by Qλ, NusA induces refolding of Qλ to form a nozzle that extends the RNA polymerase RNA-exit channel.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 119, Issue 33, Page e2205278119, Year 2022
掲載日	2022年8月16日
著者	Zhou Yin / Jeremy G Bird / Jason T Kaelber / Bryce E Nickels / Richard H Ebright /
PubMed 要旨	Lambdoid bacteriophage Q proteins are transcription antipausing and antitermination factors that enable RNA polymerase (RNAP) to read through pause and termination sites. Q proteins load onto RNAP ...Lambdoid bacteriophage Q proteins are transcription antipausing and antitermination factors that enable RNA polymerase (RNAP) to read through pause and termination sites. Q proteins load onto RNAP engaged in promoter-proximal pausing at a Q binding element (QBE) and adjacent sigma-dependent pause element to yield a Q-loading complex, and they translocate with RNAP as a pausing-deficient, termination-deficient Q-loaded complex. In previous work, we showed that the Q protein of bacteriophage 21 (Q21) functions by forming a nozzle that narrows and extends the RNAP RNA-exit channel, preventing formation of pause and termination RNA hairpins. Here, we report atomic structures of four states on the pathway of antitermination by the Q protein of bacteriophage λ (Qλ), a Q protein that shows no sequence similarity to Q21 and that, unlike Q21, requires the transcription elongation factor NusA for efficient antipausing and antitermination. We report structures of Qλ, the Qλ-QBE complex, the NusA-free pre-engaged Qλ-loading complex, and the NusA-containing engaged Qλ-loading complex. The results show that Qλ, like Q21, forms a nozzle that narrows and extends the RNAP RNA-exit channel, preventing formation of RNA hairpins. However, the results show that Qλ has no three-dimensional structural similarity to Q21, employs a different mechanism of QBE recognition than Q21, and employs a more complex process for loading onto RNAP than Q21, involving recruitment of Qλ to form a pre-engaged loading complex, followed by NusA-facilitated refolding of Qλ to form an engaged loading complex. The results establish that Qλ and Q21 are not structural homologs and are solely functional analogs.
リンク	Proc Natl Acad Sci U S A / PubMed:35951650 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.46 - 3.36 Å
構造データ	26438 7ubm EMDB-26438, PDB-7ubm: Transcription antitermination complex: "pre-engaged" Qlambda-loading complex 手法: EM (単粒子) / 解像度: 3.13 Å 26439 7ubn EMDB-26439, PDB-7ubn: Transcription antitermination complex: NusA-containing "engaged" Qlambda-loading complex 手法: EM (単粒子) / 解像度: 3.36 Å PDB-7ubj: Transcription antitermination factor Qlambda, type-I crystal 手法: X-RAY DIFFRACTION / 解像度: 1.46 Å PDB-7ubk: Transcription antitermination factor Qlambda, type-II crystal 手法: X-RAY DIFFRACTION / 解像度: 1.97 Å PDB-7ubl: Transcription antitermination factor Qlambda in complex with Q-lambda-binding-element DNA 手法: X-RAY DIFFRACTION / 解像度: 2.177 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-CL: Unknown entry / クロリド ChemComp-GOL: GLYCEROL / グリセロ-ル ChemComp-EDO: 1,2-ETHANEDIOL / エチレングリコ-ル ChemComp-PEG: DI(HYDROXYETHYL)ETHER / ジエチレングリコ-ル ChemComp-PO4: PHOSPHATE ION / ホスファ-ト ChemComp-HOH: WATER ChemComp-MG: Unknown entry / マグネシウムジカチオン
由来	escherichia coli (大腸菌) escherichia phage lambda (λファージ)
キーワード	GENE REGULATION / RNA polymerase / DNA Binding / transcription / Q-dependent antitermination / Q antitermination factor / GENE REGULATION/DNA / GENE REGULATION-DNA complex / TRANSFERASE/DNA/RNA / TRANSFERASE-DNA-RNA complex