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  An Autoinhibited State in the Structure of Thermotoga maritima NusG

Drögemueller, J., Stegmann, C. M., Mandal, A., Steiner, T., Burmann, B. M., Gottesman, M. E., et al. (2013). An Autoinhibited State in the Structure of Thermotoga maritima NusG. STRUCTURE, 21(3), 365-375. doi:10.1016/j.str.2012.12.015.

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 Creators:
Drögemueller, Johanna1, Author
Stegmann, Christian M.1, Author
Mandal, Angshuman1, Author
Steiner, Thomas2, Author              
Burmann, Björn M.1, Author
Gottesman, Max E.1, Author
Wöhrl, Birgitta M.1, Author
Rösch, Paul1, Author
Wahl, Markus C.1, Author
Schweimer, Kristian1, Author
Affiliations:
1external, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Free keywords: DEPENDENT TRANSCRIPTION TERMINATION; ESCHERICHIA-COLI NUSA; RNA-POLYMERASE; IN-VIVO; ALPHA-SUBUNIT; PHAGE-LAMBDA; N-PROTEIN; ANTITERMINATION; ELONGATION; DOMAINS
 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 coil NusG, suggesting that the NTD-CTD interaction of TmNusG represents an autoinhibited state.

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Language(s): eng - English
 Dates: 2013-03-05
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000315975100008
DOI: 10.1016/j.str.2012.12.015
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 21 (3) Sequence Number: - Start / End Page: 365 - 375 Identifier: ISSN: 0969-2126