The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling

The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling

The bacterial helicase-like transcription factor HelD interacts with the RNA polymerase (RNAP) and together with the RNAP δ subunit enhances RNAP cycling. Here, the authors present the cryo-EM structures of the monomeric and dimeric Bacillus subtilis RNAP-δ-HelD complexes and suggest a model for Hel...

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Autores principales: Hao-Hong Pei, Tarek Hilal, Zhuo A. Chen, Yong-Heng Huang, Yuan Gao, Nelly Said, Bernhard Loll, Juri Rappsilber, Georgiy A. Belogurov, Irina Artsimovitch, Markus C. Wahl
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Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/862de4900b514335855420b64fe9f8ae
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spelling oai:doaj.org-article:862de4900b514335855420b64fe9f8ae2021-12-02T10:48:28ZThe δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling10.1038/s41467-020-20159-32041-1723https://doaj.org/article/862de4900b514335855420b64fe9f8ae2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20159-3https://doaj.org/toc/2041-1723The bacterial helicase-like transcription factor HelD interacts with the RNA polymerase (RNAP) and together with the RNAP δ subunit enhances RNAP cycling. Here, the authors present the cryo-EM structures of the monomeric and dimeric Bacillus subtilis RNAP-δ-HelD complexes and suggest a model for HelD/δ-mediated RNAP recycling and putative hibernation.Hao-Hong PeiTarek HilalZhuo A. ChenYong-Heng HuangYuan GaoNelly SaidBernhard LollJuri RappsilberGeorgiy A. BelogurovIrina ArtsimovitchMarkus C. WahlNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Hao-Hong Pei
Tarek Hilal
Zhuo A. Chen
Yong-Heng Huang
Yuan Gao
Nelly Said
Bernhard Loll
Juri Rappsilber
Georgiy A. Belogurov
Irina Artsimovitch
Markus C. Wahl
The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
description The bacterial helicase-like transcription factor HelD interacts with the RNA polymerase (RNAP) and together with the RNAP δ subunit enhances RNAP cycling. Here, the authors present the cryo-EM structures of the monomeric and dimeric Bacillus subtilis RNAP-δ-HelD complexes and suggest a model for HelD/δ-mediated RNAP recycling and putative hibernation.
format article
author Hao-Hong Pei
Tarek Hilal
Zhuo A. Chen
Yong-Heng Huang
Yuan Gao
Nelly Said
Bernhard Loll
Juri Rappsilber
Georgiy A. Belogurov
Irina Artsimovitch
Markus C. Wahl
author_facet Hao-Hong Pei
Tarek Hilal
Zhuo A. Chen
Yong-Heng Huang
Yuan Gao
Nelly Said
Bernhard Loll
Juri Rappsilber
Georgiy A. Belogurov
Irina Artsimovitch
Markus C. Wahl
author_sort Hao-Hong Pei
title The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
title_short The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
title_full The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
title_fullStr The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
title_full_unstemmed The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
title_sort δ subunit and ntpase held institute a two-pronged mechanism for rna polymerase recycling
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/862de4900b514335855420b64fe9f8ae
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