Cargando…
Structural mechanism of ATP-independent transcription initiation by RNA polymerase I
Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a structure of Saccharomyces cerevisiae Pol I-CF-DNA to 3.8 Å resolution using single-particle cryo-electro...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5489313/ https://www.ncbi.nlm.nih.gov/pubmed/28623663 http://dx.doi.org/10.7554/eLife.27414 |
_version_ | 1783246776972607488 |
---|---|
author | Han, Yan Yan, Chunli Nguyen, Thi Hoang Duong Jackobel, Ashleigh J Ivanov, Ivaylo Knutson, Bruce A He, Yuan |
author_facet | Han, Yan Yan, Chunli Nguyen, Thi Hoang Duong Jackobel, Ashleigh J Ivanov, Ivaylo Knutson, Bruce A He, Yuan |
author_sort | Han, Yan |
collection | PubMed |
description | Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a structure of Saccharomyces cerevisiae Pol I-CF-DNA to 3.8 Å resolution using single-particle cryo-electron microscopy. The structure reveals a bipartite architecture of Core Factor and its recognition of the promoter from −27 to −16. Core Factor’s intrinsic mobility correlates well with different conformational states of the Pol I cleft, in addition to the stabilization of either Rrn7 N-terminal domain near Pol I wall or the tandem winged helix domain of A49 at a partially overlapping location. Comparison of the three states in this study with the Pol II system suggests that a ratchet motion of the Core Factor-DNA sub-complex at upstream facilitates promoter melting in an ATP-independent manner, distinct from a DNA translocase actively threading the downstream DNA in the Pol II PIC. DOI: http://dx.doi.org/10.7554/eLife.27414.001 |
format | Online Article Text |
id | pubmed-5489313 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-54893132017-06-30 Structural mechanism of ATP-independent transcription initiation by RNA polymerase I Han, Yan Yan, Chunli Nguyen, Thi Hoang Duong Jackobel, Ashleigh J Ivanov, Ivaylo Knutson, Bruce A He, Yuan eLife Biophysics and Structural Biology Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a structure of Saccharomyces cerevisiae Pol I-CF-DNA to 3.8 Å resolution using single-particle cryo-electron microscopy. The structure reveals a bipartite architecture of Core Factor and its recognition of the promoter from −27 to −16. Core Factor’s intrinsic mobility correlates well with different conformational states of the Pol I cleft, in addition to the stabilization of either Rrn7 N-terminal domain near Pol I wall or the tandem winged helix domain of A49 at a partially overlapping location. Comparison of the three states in this study with the Pol II system suggests that a ratchet motion of the Core Factor-DNA sub-complex at upstream facilitates promoter melting in an ATP-independent manner, distinct from a DNA translocase actively threading the downstream DNA in the Pol II PIC. DOI: http://dx.doi.org/10.7554/eLife.27414.001 eLife Sciences Publications, Ltd 2017-06-17 /pmc/articles/PMC5489313/ /pubmed/28623663 http://dx.doi.org/10.7554/eLife.27414 Text en © 2017, Han et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Biophysics and Structural Biology Han, Yan Yan, Chunli Nguyen, Thi Hoang Duong Jackobel, Ashleigh J Ivanov, Ivaylo Knutson, Bruce A He, Yuan Structural mechanism of ATP-independent transcription initiation by RNA polymerase I |
title | Structural mechanism of ATP-independent transcription initiation by RNA polymerase I |
title_full | Structural mechanism of ATP-independent transcription initiation by RNA polymerase I |
title_fullStr | Structural mechanism of ATP-independent transcription initiation by RNA polymerase I |
title_full_unstemmed | Structural mechanism of ATP-independent transcription initiation by RNA polymerase I |
title_short | Structural mechanism of ATP-independent transcription initiation by RNA polymerase I |
title_sort | structural mechanism of atp-independent transcription initiation by rna polymerase i |
topic | Biophysics and Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5489313/ https://www.ncbi.nlm.nih.gov/pubmed/28623663 http://dx.doi.org/10.7554/eLife.27414 |
work_keys_str_mv | AT hanyan structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei AT yanchunli structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei AT nguyenthihoangduong structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei AT jackobelashleighj structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei AT ivanovivaylo structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei AT knutsonbrucea structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei AT heyuan structuralmechanismofatpindependenttranscriptioninitiationbyrnapolymerasei |