ArticleStructure (London, England : 1993)2013
An autoinhibited state in the structure of Thermotoga maritima NusG.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Evolutionary selection of proteins with two folds.bioRxiv : the preprint server for biology · 2023Article
- Many dissimilar NusG protein domains switch between α-helix and β-sheet folds.Nature communications · 2022Article
- Article
- NusG, an Ancient Yet Rapidly Evolving Transcription Factor.Frontiers in microbiology · 2020Review
- Reversible fold-switching controls the functional cycle of the antitermination factor RfaH.Nature communications · 2019Article
- Structure and nucleic acid binding properties of KOW domains 4 and 6-7 of human transcription elongation factor DSIF.Scientific reports · 2018Article
- Thermotoga maritima NusG: domain interaction mediates autoinhibition and thermostability.Nucleic acids research · 2017Article
- Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape.PLoS computational biology · 2015Article
- Ubiquitous transcription factors display structural plasticity and diverse functions: NusG proteins - Shifting shapes and paradigms.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- Interdomain contacts control folding of transcription factor RfaH.Nucleic acids research · 2013Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
NusG is a conserved regulatory protein interacting with RNA polymerase (RNAP) and other proteins to form multicomponent complexes that modulate transcription. The crystal structure of Thermotoga maritima NusG (TmNusG) shows a three-domain architecture, comprising well-conserved amino-terminal (NTD) and carboxy-terminal (CTD) domains with an additional, species-specific domain inserted into the NTD. NTD and CTD directly contact each other, occluding a surface of the NTD for binding to RNAP and a surface on the CTD interacting either with transcription termination factor Rho or transcription antitermination factor NusE. NMR spectroscopy confirmed the intramolecular NTD-CTD interaction up to the optimal growth temperature of Thermotoga maritima. The domain interaction involves a dynamic equilibrium between open and closed states and contributes significantly to the overall fold stability of the protein. Wild-type TmNusG and deletion variants could not replace endogenous Escherichia coli NusG, suggesting that the NTD-CTD interaction of TmNusG represents an autoinhibited state.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.