title: An autoinhibited state in the structure of Thermotoga maritima NusG.
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.
authors: Lehrstuhl Biopolymere und Forschungszentrum für Biomakromoleküle, Universität Bayreuth, Universitätsstrasse 30, Bayreuth, Germany.
authors: Johanna
authors: J
authors: Drögemüller
authors: Christian M
authors: CM
authors: Stegmann
authors: Angshuman
authors: A
authors: Mandal
authors: Thomas
authors: T
authors: Steiner
authors: Björn M
authors: BM
authors: Burmann
authors: Max E
authors: ME
authors: Gottesman
authors: Birgitta M
authors: BM
authors: Wöhrl
authors: Paul
authors: P
authors: Rösch
authors: Markus C
authors: MC
authors: Wahl
authors: Kristian
authors: K
authors: Schweimer
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D018360:Crystallography, X-Ray; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000235:genetics; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000254:growth & development; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D005816:Genetic Complementation Test; D056004:Molecular Dynamics Simulation; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000235:genetics; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012234:Rho Factor / Q000737:chemistry / Q000235:genetics; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics; D013045:Species Specificity; D013329:Structure-Activity Relationship; D020124:Thermotoga maritima / Q000737:chemistry* / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C070291:NusG protein, E coli; D010445:Peptide Elongation Factors; D011994:Recombinant Proteins; D012234:Rho Factor; D012269:Ribosomal Proteins; D014157:Transcription Factors; C029537:ribosomal protein S10; D012321:DNA-Directed RNA Polymerases