The bacterial transcription factor NusG (N-utilization substance G) is suggested to act as a key coupling factor between transcription and translation [Burmann, Schweimer, Luo, Wahl, Stitt, Gottesman and Rösch (2010) Science 328, 501–504] and contributes to phage λ-mediated antitermination in Escherichia coli that enables read-through of early transcription termination sites. E. coli NusG consists of two structurally and functionally distinct domains that are connected through a flexible linker. The homologous Aquifex aeolicus NusG, with a secondary structure that is highly similar to E. coli NusG shows direct interaction between its N- and C-terminal domains in a domain-swapped dimer. In the present study, we performed NMR paramagnetic relaxation enhancement measurements and identified interdomain interactions that were concentration dependent and thus probably not only weak and transient, but also predominantly intermolecular. This notion of two virtually independent domains in a monomeric protein was supported by 15N-relaxation measurements. Thus we suggest that a regulatory role of NusG interdomain interactions is highly unlikely.
Skip Nav Destination
Article navigation
May 2011
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Research Article|
April 13 2011
Domain interactions of the transcription–translation coupling factor Escherichia coli NusG are intermolecular and transient
Björn M. Burmann;
Björn M. Burmann
1Lehrstuhl für Biopolymere and Research Centre for Biomacromolecules, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany
Search for other works by this author on:
Ulrich Scheckenhofer;
Ulrich Scheckenhofer
1Lehrstuhl für Biopolymere and Research Centre for Biomacromolecules, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany
Search for other works by this author on:
Kristian Schweimer;
Kristian Schweimer
1Lehrstuhl für Biopolymere and Research Centre for Biomacromolecules, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany
Search for other works by this author on:
Paul Rösch
Paul Rösch
1
1Lehrstuhl für Biopolymere and Research Centre for Biomacromolecules, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany
1To whom correspondence should be addressed (email roesch@unibt.de).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
October 13 2010
Revision Received:
February 02 2011
Accepted:
February 23 2011
Accepted Manuscript online:
February 23 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem J (2011) 435 (3): 783–789.
Article history
Received:
October 13 2010
Revision Received:
February 02 2011
Accepted:
February 23 2011
Accepted Manuscript online:
February 23 2011
Citation
Björn M. Burmann, Ulrich Scheckenhofer, Kristian Schweimer, Paul Rösch; Domain interactions of the transcription–translation coupling factor Escherichia coli NusG are intermolecular and transient. Biochem J 1 May 2011; 435 (3): 783–789. doi: https://doi.org/10.1042/BJ20101679
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.