Direct binding of TFEα opens DNA binding cleft of RNA polymerase

How clamp conformation is regulated in the transcription cycle of stalk-containing archaeal and eukaryotic RNA polymerase (RNAP) systems is still not well understood. Here, the authors combine cryo-EM, X-ray crystallography and photo-crosslinking assays to structurally characterise RNAP, the RNAP-TF...

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Autores principales: Sung-Hoon Jun, Jaekyung Hyun, Jeong Seok Cha, Hoyoung Kim, Michael S. Bartlett, Hyun-Soo Cho, Katsuhiko S. Murakami
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/9ace4ca1aed44741b400bd87ec0e18c7
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spelling oai:doaj.org-article:9ace4ca1aed44741b400bd87ec0e18c72021-12-02T15:37:16ZDirect binding of TFEα opens DNA binding cleft of RNA polymerase10.1038/s41467-020-19998-x2041-1723https://doaj.org/article/9ace4ca1aed44741b400bd87ec0e18c72020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19998-xhttps://doaj.org/toc/2041-1723How clamp conformation is regulated in the transcription cycle of stalk-containing archaeal and eukaryotic RNA polymerase (RNAP) systems is still not well understood. Here, the authors combine cryo-EM, X-ray crystallography and photo-crosslinking assays to structurally characterise RNAP, the RNAP-TFEα binary and RNAP-TFEα-promoter DNA ternary complexes from the archaea Thermococcus kodakarensis and enables them to describe the dynamic conformational changes of the general transcription factor TFEα and RNAP during the early stage of transcription cycle.Sung-Hoon JunJaekyung HyunJeong Seok ChaHoyoung KimMichael S. BartlettHyun-Soo ChoKatsuhiko S. MurakamiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Sung-Hoon Jun
Jaekyung Hyun
Jeong Seok Cha
Hoyoung Kim
Michael S. Bartlett
Hyun-Soo Cho
Katsuhiko S. Murakami
Direct binding of TFEα opens DNA binding cleft of RNA polymerase
description How clamp conformation is regulated in the transcription cycle of stalk-containing archaeal and eukaryotic RNA polymerase (RNAP) systems is still not well understood. Here, the authors combine cryo-EM, X-ray crystallography and photo-crosslinking assays to structurally characterise RNAP, the RNAP-TFEα binary and RNAP-TFEα-promoter DNA ternary complexes from the archaea Thermococcus kodakarensis and enables them to describe the dynamic conformational changes of the general transcription factor TFEα and RNAP during the early stage of transcription cycle.
format article
author Sung-Hoon Jun
Jaekyung Hyun
Jeong Seok Cha
Hoyoung Kim
Michael S. Bartlett
Hyun-Soo Cho
Katsuhiko S. Murakami
author_facet Sung-Hoon Jun
Jaekyung Hyun
Jeong Seok Cha
Hoyoung Kim
Michael S. Bartlett
Hyun-Soo Cho
Katsuhiko S. Murakami
author_sort Sung-Hoon Jun
title Direct binding of TFEα opens DNA binding cleft of RNA polymerase
title_short Direct binding of TFEα opens DNA binding cleft of RNA polymerase
title_full Direct binding of TFEα opens DNA binding cleft of RNA polymerase
title_fullStr Direct binding of TFEα opens DNA binding cleft of RNA polymerase
title_full_unstemmed Direct binding of TFEα opens DNA binding cleft of RNA polymerase
title_sort direct binding of tfeα opens dna binding cleft of rna polymerase
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/9ace4ca1aed44741b400bd87ec0e18c7
work_keys_str_mv AT sunghoonjun directbindingoftfeaopensdnabindingcleftofrnapolymerase
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AT hoyoungkim directbindingoftfeaopensdnabindingcleftofrnapolymerase
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