Document Detail


An autoinhibited state in the structure of Thermotoga maritima NusG.
MedLine Citation:
PMID:  23415559     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Johanna Drögemüller; Christian M Stegmann; Angshuman Mandal; Thomas Steiner; Björn M Burmann; Max E Gottesman; Birgitta M Wöhrl; Paul Rösch; Markus C Wahl; Kristian Schweimer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-02-14
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  21     ISSN:  1878-4186     ISO Abbreviation:  Structure     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-11     Completed Date:  2013-08-16     Revised Date:  2014-03-06    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  United States    
Other Details:
Languages:  eng     Pagination:  365-75     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 Elsevier Ltd. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / chemistry*,  genetics
Binding Sites
Crystallography, X-Ray
DNA-Directed RNA Polymerases / chemistry,  genetics
Escherichia coli / chemistry,  genetics,  growth & development
Escherichia coli Proteins / chemistry*,  genetics
Genetic Complementation Test
Molecular Dynamics Simulation
Peptide Elongation Factors / chemistry*,  genetics
Protein Binding
Protein Interaction Domains and Motifs
Protein Stability
Protein Structure, Secondary
Recombinant Proteins / chemistry,  genetics
Rho Factor / chemistry,  genetics
Ribosomal Proteins / chemistry,  genetics
Species Specificity
Structure-Activity Relationship
Thermotoga maritima / chemistry*,  genetics
Transcription Factors / chemistry*,  genetics
Grant Support
ID/Acronym/Agency:
R01 GM037219/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/NusG protein, E coli; 0/Peptide Elongation Factors; 0/Recombinant Proteins; 0/Rho Factor; 0/Ribosomal Proteins; 0/Transcription Factors; 0/ribosomal protein S10; EC 2.7.7.6/DNA-Directed RNA Polymerases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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