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Mechanisms of DNA opening revealed in AAA+ transcription complex structures
Gene transcription is carried out by RNA polymerase (RNAP) and requires the conversion of the initial closed promoter complex, where DNA is double stranded, to a transcription-competent open promoter complex, where DNA is opened up. In bacteria, RNAP relies on σ factors for its promoter specificitie...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9770992/ https://www.ncbi.nlm.nih.gov/pubmed/36542713 http://dx.doi.org/10.1126/sciadv.add3479 |
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author | Ye, Fuzhou Gao, Forson Liu, Xiaojiao Buck, Martin Zhang, Xiaodong |
author_facet | Ye, Fuzhou Gao, Forson Liu, Xiaojiao Buck, Martin Zhang, Xiaodong |
author_sort | Ye, Fuzhou |
collection | PubMed |
description | Gene transcription is carried out by RNA polymerase (RNAP) and requires the conversion of the initial closed promoter complex, where DNA is double stranded, to a transcription-competent open promoter complex, where DNA is opened up. In bacteria, RNAP relies on σ factors for its promoter specificities. Using a special form of sigma factor (σ(54)), which forms a stable closed complex and requires its activator that belongs to the AAA+ ATPases (ATPases associated with diverse cellular activities), we obtained cryo–electron microscopy structures of transcription initiation complexes that reveal a previously unidentified process of DNA melting opening. The σ(54) amino terminus threads through the locally opened up DNA and then becomes enclosed by the AAA+ hexameric ring in the activator-bound intermediate complex. Our structures suggest how ATP hydrolysis by the AAA+ activator could remove the σ(54) inhibition while helping to open up DNA, using σ(54) amino-terminal peptide as a pry bar. |
format | Online Article Text |
id | pubmed-9770992 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-97709922022-12-28 Mechanisms of DNA opening revealed in AAA+ transcription complex structures Ye, Fuzhou Gao, Forson Liu, Xiaojiao Buck, Martin Zhang, Xiaodong Sci Adv Biomedicine and Life Sciences Gene transcription is carried out by RNA polymerase (RNAP) and requires the conversion of the initial closed promoter complex, where DNA is double stranded, to a transcription-competent open promoter complex, where DNA is opened up. In bacteria, RNAP relies on σ factors for its promoter specificities. Using a special form of sigma factor (σ(54)), which forms a stable closed complex and requires its activator that belongs to the AAA+ ATPases (ATPases associated with diverse cellular activities), we obtained cryo–electron microscopy structures of transcription initiation complexes that reveal a previously unidentified process of DNA melting opening. The σ(54) amino terminus threads through the locally opened up DNA and then becomes enclosed by the AAA+ hexameric ring in the activator-bound intermediate complex. Our structures suggest how ATP hydrolysis by the AAA+ activator could remove the σ(54) inhibition while helping to open up DNA, using σ(54) amino-terminal peptide as a pry bar. American Association for the Advancement of Science 2022-12-21 /pmc/articles/PMC9770992/ /pubmed/36542713 http://dx.doi.org/10.1126/sciadv.add3479 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Ye, Fuzhou Gao, Forson Liu, Xiaojiao Buck, Martin Zhang, Xiaodong Mechanisms of DNA opening revealed in AAA+ transcription complex structures |
title | Mechanisms of DNA opening revealed in AAA+ transcription complex structures |
title_full | Mechanisms of DNA opening revealed in AAA+ transcription complex structures |
title_fullStr | Mechanisms of DNA opening revealed in AAA+ transcription complex structures |
title_full_unstemmed | Mechanisms of DNA opening revealed in AAA+ transcription complex structures |
title_short | Mechanisms of DNA opening revealed in AAA+ transcription complex structures |
title_sort | mechanisms of dna opening revealed in aaa+ transcription complex structures |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9770992/ https://www.ncbi.nlm.nih.gov/pubmed/36542713 http://dx.doi.org/10.1126/sciadv.add3479 |
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