Abstract
NusA and NusG are major regulators of bacterial transcription elongation, which act either in concert or antagonistically. Both bind to RNA polymerase (RNAP), regulating pausing as well as intrinsic and Rho-dependent termination. Here, we demonstrate by nuclear magnetic resonance spectroscopy that the Escherichia coli NusG amino-terminal domain forms a complex with the acidic repeat domain 2 (AR2) of NusA. The interaction surface of either transcription factor overlaps with the respective binding site for RNAP. We show that NusA-AR2 is able to remove NusG from RNAP. Our in vivo and in vitro results suggest that interaction between NusA and NusG could play various regulatory roles during transcription, including recruitment of NusG to RNAP, resynchronization of transcription:translation coupling, and modulation of termination efficiency.
© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.
MeSH terms
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Binding Sites
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DNA-Directed RNA Polymerases / genetics*
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DNA-Directed RNA Polymerases / metabolism
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / metabolism
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Gene Expression Regulation, Bacterial*
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Molecular Docking Simulation
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Nuclear Magnetic Resonance, Biomolecular
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Peptide Elongation Factors / chemistry
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Peptide Elongation Factors / genetics*
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Peptide Elongation Factors / metabolism
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Protein Binding
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Protein Domains
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Protein Structure, Secondary
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Transcription Factors / chemistry
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Transcription Factors / genetics*
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Transcription Factors / metabolism
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Transcription, Genetic*
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Transcriptional Elongation Factors / chemistry
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Transcriptional Elongation Factors / genetics*
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Transcriptional Elongation Factors / metabolism
Substances
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Escherichia coli Proteins
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NusG protein, E coli
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Peptide Elongation Factors
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Transcription Factors
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Transcriptional Elongation Factors
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nusA protein, E coli
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DNA-Directed RNA Polymerases