4.8 Article

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

Journal

NUCLEIC ACIDS RESEARCH
Volume 43, Issue 2, Pages 1133-1146

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/nar/gku1370

Keywords

-

Funding

  1. National Institutes of Health [GM092949, NIH GM092949]
  2. National Science Foundation [MCB 1050867]
  3. XSEDE [TG-MCB090003, TG-MCB120005]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

Article Biochemistry & Molecular Biology

Mutational and Computational Evidence That a Nickel-Transfer Tunnel in UreD Is Used for Activation of Klebsiella aerogenes Urease

Mark A. Farrugia, Beibei Wang, Michael Feig, Robert P. Hausinger

BIOCHEMISTRY (2015)

Meeting Abstract Biophysics

Alternative Base-Pairing and Conformational Sampling in Loop a of the Hairpin Ribozyme

Patrick O. Ochieng, Beibei Wang, Michael Feig, Charles G. Hoogstraten

BIOPHYSICAL JOURNAL (2015)

Article Multidisciplinary Sciences

Stepwise substrate translocation mechanism revealed by free energy calculations of doxorubicin in the multidrug transporter AcrB

Zhicheng Zuo, Beibei Wang, Jingwei Weng, Wenning Wang

SCIENTIFIC REPORTS (2015)

Meeting Abstract Biophysics

Long-Range Allosteric Communication in Muts and Homologs via Molecular Dynamics Simulations

Michael Feig, Beibei Wang, Joshua Francis

BIOPHYSICAL JOURNAL (2016)

Article Biochemical Research Methods

Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication Pathways

Beibei Wang, Joshua Francis, Monika Sharma, Sean M. Law, Alexander V. Predeus, Michael Feig

PLOS COMPUTATIONAL BIOLOGY (2016)

Article Biophysics

Energetic and Structural Details of the Trigger-Loop Closing Transition in RNA Polymerase II

Beibei Wang, Alexander V. Predeus, Zachary F. Burton, Michael Feig

BIOPHYSICAL JOURNAL (2013)

Review Chemistry, Multidisciplinary

Computational Simulation Strategies for Analysis of Multisubunit RNA Polymerases

Beibei Wang, Michael Feig, Robert I. Cukier, Zachary F. Burton

CHEMICAL REVIEWS (2013)

Article Chemistry, Physical

Interdomain Flexibility and pH-Induced Conformational Changes of AcrA Revealed by Molecular Dynamics Simulations

Beibei Wang, Jingwei Weng, Kangnian Fan, Wenning Wang

JOURNAL OF PHYSICAL CHEMISTRY B (2012)

Article Biochemistry & Molecular Biology

Elastic network model-based normal mode analysis reveals the conformational couplings in the tripartite AcrAB-TolC multidrug efflux complex

Beibei Wang, Jingwei Weng, Kangnian Fan, Wenning Wang

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2011)

Article Biochemistry & Molecular Biology

Multiple conformational states and gate opening of outer membrane protein ToIC revealed by molecular dynamics simulations

Beibei Wang, Jingwei Weng, Wenning Wang

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2014)

Letter Hematology

Ectopic ATP synthase β subunit proteins on human leukemia cell surface interact with platelets by binding glycoprotein IIb

Ting Wang, Ying Shen, Yuanyuan Li, Beibei Wang, Benfang Wang, Depei Wu, Changgeng Ruan, Yiqiang Wang

HAEMATOLOGICA (2019)

Article Microbiology

BioMaster: An Integrated Database and Analytic Platform to Provide Comprehensive Information About BioBrick Parts

Beibei Wang, Huayi Yang, Jianan Sun, Chuhao Dou, Jian Huang, Feng-Biao Guo

Summary: Synthetic biology aims to create new biological parts, devices, and systems, and reconfigure existing natural biological systems. The development of the BioMaster database complements information about BioBrick parts extensively and provides a user-friendly platform for retrieval and analysis.

FRONTIERS IN MICROBIOLOGY (2021)

No Data Available