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Thermotoga maritima NusG : domain interaction mediates autoinhibition and thermostability

Titelangaben

Drögemüller, Johanna ; Schneider, Christin ; Schweimer, Kristian ; Strauß, Martin ; Wöhrl, Birgitta M. ; Rösch, Paul ; Knauer, Stefan H.:
Thermotoga maritima NusG : domain interaction mediates autoinhibition and thermostability.
In: Nucleic Acids Research. Bd. 45 (2017) Heft 1 . - S. 446-460.
ISSN 1362-4962
DOI: 10.1093/nar/gkw1111

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Projektfinanzierung: Andere

Abstract

NusG, the only universally conserved transcription factor, comprises an N- and a C-terminal domain (NTD, CTD) that are flexibly connected and move in- dependently in Escherichia coli and other organisms. In NusG from the hyperthermophilic bacterium Thermotoga maritima (tmNusG), however, NTD and CTD interact tightly. This closed state stabilizes the CTD, but masks the binding sites for the interaction partners Rho, NusE and RNA polymerase (RNAP), suggesting that tmNusG is autoinhibited. Furthermore, tmNusG and some other bacterial NusGs have an additional domain, DII, of unknown function. Here we demonstrate that tmNusG is indeed autoinhibited and that binding to RNAP may stabilize the open conformation. We identified two interdomain salt bridges as well as Phe336 as major determinants of the domain interaction. By successive weakening of this interaction we show that after domain dissociation tmNusG-CTD can bind to Rho and NusE, similar to the Escherichia coli NusG-CTD, indicating that these interactions are conserved in bacteria. Furthermore, we show that tmNusG-DII interacts with RNAP as well as nucleic acids with a clear preference for double stranded DNA. We suggest that tmNusG-DII supports tmNusG recruitment to the transcription elongation complex and stabilizes the tmNusG:RNAP complex, a necessary adaptation to high temperatures.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biopolymere
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biopolymere > Lehrstuhl Biopolymere - Univ.-Prof. Dr. Paul Rösch
Profilfelder
Profilfelder > Advanced Fields
Profilfelder > Advanced Fields > Polymer- und Kolloidforschung
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 500 Naturwissenschaften
500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 03 Mai 2017 07:05
Letzte Änderung: 03 Mai 2017 07:05
URI: https://eref.uni-bayreuth.de/id/eprint/36915