Document Detail

An autoinhibited state in the structure of Thermotoga maritima NusG.
MedLine Citation:
PMID:  23415559     Owner:  NLM     Status:  MEDLINE    
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.
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
Related Documents :
23650599 - Extended c-terminus and length of the linker connecting the g-domains are species-speci...
2040429 - Penicillin-binding protein 4 of escherichia coli shows a novel type of primary structur...
24466279 - Cloning and characterization of a 7 transmembrane receptor from the adherent cells of c...
24651689 - A compact, multifunctional fusion module directs cholesterol-dependent homomultimerizat...
24391959 - Putative sugar transporters of the mustard leaf beetle phaedon cochleariae: their phylo...
24257609 - Bovine ephemeral fever rhabdovirus α1 protein has viroporin-like properties and binds i...
12193299 - Cross-reactivity of a monoclonal antibody to the amino terminal region of thyrotropin r...
4598289 - Activity of colicin e3-treated ribosomes in initiation and in chain elongation.
22645569 - The nucleocapsid protein of potato yellow dwarf virus: protein interactions and nuclear...
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.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
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
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 RNA Polymerases

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

Previous Document:  Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties...
Next Document:  Hypothermia for acute ischaemic stroke.