Structural basis of Q-dependent transcription antitermination

Bacteriophage Q protein serves as a model regulator for the study of transcription elongation. Here the authors report a cryo-EM structure of an intact Q-engaged arrested complex, revealing the interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jing Shi, Xiang Gao, Tongguan Tian, Zhaoyang Yu, Bo Gao, Aijia Wen, Linlin You, Shenghai Chang, Xing Zhang, Yu Zhang, Yu Feng
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7e9689354b724ad5a73fd6c510dd9e7b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:7e9689354b724ad5a73fd6c510dd9e7b
record_format	dspace
spelling	oai:doaj.org-article:7e9689354b724ad5a73fd6c510dd9e7b2021-12-02T15:35:55ZStructural basis of Q-dependent transcription antitermination10.1038/s41467-019-10958-82041-1723https://doaj.org/article/7e9689354b724ad5a73fd6c510dd9e7b2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10958-8https://doaj.org/toc/2041-1723Bacteriophage Q protein serves as a model regulator for the study of transcription elongation. Here the authors report a cryo-EM structure of an intact Q-engaged arrested complex, revealing the interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination.Jing ShiXiang GaoTongguan TianZhaoyang YuBo GaoAijia WenLinlin YouShenghai ChangXing ZhangYu ZhangYu FengNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jing Shi Xiang Gao Tongguan Tian Zhaoyang Yu Bo Gao Aijia Wen Linlin You Shenghai Chang Xing Zhang Yu Zhang Yu Feng Structural basis of Q-dependent transcription antitermination
description	Bacteriophage Q protein serves as a model regulator for the study of transcription elongation. Here the authors report a cryo-EM structure of an intact Q-engaged arrested complex, revealing the interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination.
format	article
author	Jing Shi Xiang Gao Tongguan Tian Zhaoyang Yu Bo Gao Aijia Wen Linlin You Shenghai Chang Xing Zhang Yu Zhang Yu Feng
author_facet	Jing Shi Xiang Gao Tongguan Tian Zhaoyang Yu Bo Gao Aijia Wen Linlin You Shenghai Chang Xing Zhang Yu Zhang Yu Feng
author_sort	Jing Shi
title	Structural basis of Q-dependent transcription antitermination
title_short	Structural basis of Q-dependent transcription antitermination
title_full	Structural basis of Q-dependent transcription antitermination
title_fullStr	Structural basis of Q-dependent transcription antitermination
title_full_unstemmed	Structural basis of Q-dependent transcription antitermination
title_sort	structural basis of q-dependent transcription antitermination
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/7e9689354b724ad5a73fd6c510dd9e7b
work_keys_str_mv	AT jingshi structuralbasisofqdependenttranscriptionantitermination AT xianggao structuralbasisofqdependenttranscriptionantitermination AT tongguantian structuralbasisofqdependenttranscriptionantitermination AT zhaoyangyu structuralbasisofqdependenttranscriptionantitermination AT bogao structuralbasisofqdependenttranscriptionantitermination AT aijiawen structuralbasisofqdependenttranscriptionantitermination AT linlinyou structuralbasisofqdependenttranscriptionantitermination AT shenghaichang structuralbasisofqdependenttranscriptionantitermination AT xingzhang structuralbasisofqdependenttranscriptionantitermination AT yuzhang structuralbasisofqdependenttranscriptionantitermination AT yufeng structuralbasisofqdependenttranscriptionantitermination
_version_	1718386422656794624

Structural basis of Q-dependent transcription antitermination

Ejemplares similares