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Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details

Transcriptional fidelity, which prevents the misincorporation of incorrect nucleoside monophosphates in RNA, is essential for life. Results from molecular dynamics (MD) simulations of eukaryotic RNA polymerase (RNAP) II and bacterial RNAP with experimental data suggest that fidelity may involve as m...

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Autores principales: Wang, Beibei, Opron, Kristopher, Burton, Zachary F., Cukier, Robert I., Feig, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4333413/
https://www.ncbi.nlm.nih.gov/pubmed/25550432
http://dx.doi.org/10.1093/nar/gku1370
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author Wang, Beibei
Opron, Kristopher
Burton, Zachary F.
Cukier, Robert I.
Feig, Michael
author_facet Wang, Beibei
Opron, Kristopher
Burton, Zachary F.
Cukier, Robert I.
Feig, Michael
author_sort Wang, Beibei
collection PubMed
description Transcriptional fidelity, which prevents the misincorporation of incorrect nucleoside monophosphates in RNA, is essential for life. Results from molecular dynamics (MD) simulations of eukaryotic RNA polymerase (RNAP) II and bacterial RNAP with experimental data suggest that fidelity may involve as many as five checkpoints. Using MD simulations, the effects of different active site NTPs in both open and closed trigger loop (TL) structures of RNAPs are compared. Unfavorable initial binding of mismatched substrates in the active site with an open TL is proposed to be the first fidelity checkpoint. The leaving of an incorrect substrate is much easier than a correct one energetically from the umbrella sampling simulations. Then, the closing motion of the TL, required for catalysis, is hindered by the presence of mismatched NTPs. Mismatched NTPs also lead to conformational changes in the active site, which perturb the coordination of magnesium ions and likely affect the ability to proceed with catalysis. This step appears to be the most important checkpoint for deoxy-NTP discrimination. Finally, structural perturbations in the template DNA and the nascent RNA in the presence of mismatches likely hinder nucleotide addition and provide the structural foundation for backtracking followed by removing erroneously incorporated nucleotides during proofreading.
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spelling pubmed-43334132015-03-18 Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details Wang, Beibei Opron, Kristopher Burton, Zachary F. Cukier, Robert I. Feig, Michael Nucleic Acids Res Nucleic Acid Enzymes Transcriptional fidelity, which prevents the misincorporation of incorrect nucleoside monophosphates in RNA, is essential for life. Results from molecular dynamics (MD) simulations of eukaryotic RNA polymerase (RNAP) II and bacterial RNAP with experimental data suggest that fidelity may involve as many as five checkpoints. Using MD simulations, the effects of different active site NTPs in both open and closed trigger loop (TL) structures of RNAPs are compared. Unfavorable initial binding of mismatched substrates in the active site with an open TL is proposed to be the first fidelity checkpoint. The leaving of an incorrect substrate is much easier than a correct one energetically from the umbrella sampling simulations. Then, the closing motion of the TL, required for catalysis, is hindered by the presence of mismatched NTPs. Mismatched NTPs also lead to conformational changes in the active site, which perturb the coordination of magnesium ions and likely affect the ability to proceed with catalysis. This step appears to be the most important checkpoint for deoxy-NTP discrimination. Finally, structural perturbations in the template DNA and the nascent RNA in the presence of mismatches likely hinder nucleotide addition and provide the structural foundation for backtracking followed by removing erroneously incorporated nucleotides during proofreading. Oxford University Press 2015-01-30 2014-12-30 /pmc/articles/PMC4333413/ /pubmed/25550432 http://dx.doi.org/10.1093/nar/gku1370 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Nucleic Acid Enzymes
Wang, Beibei
Opron, Kristopher
Burton, Zachary F.
Cukier, Robert I.
Feig, Michael
Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details
title Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details
title_full Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details
title_fullStr Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details
title_full_unstemmed Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details
title_short Five checkpoints maintaining the fidelity of transcription by RNA polymerases in structural and energetic details
title_sort five checkpoints maintaining the fidelity of transcription by rna polymerases in structural and energetic details
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4333413/
https://www.ncbi.nlm.nih.gov/pubmed/25550432
http://dx.doi.org/10.1093/nar/gku1370
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