Berglechner, F. and Richter, G. and Fischer, M. and Bacher, A. and Gschwind, R. M. and Huenges, M. and Gemmecker, G. and Kessler, H. (1997) Studies on the NusB protein of Escherichia coli; Expression and determination of the secondary structure elements by multinuclear NMR spectroscopy. European Journal of Biochemistry 248 (2), pp. 338-346.
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The product of the nusB gene of Escherichia coli modulates the efficiency of transcription termination at I Z M ~(N utilization) sites of various bacterial and bacteriophage i genes. Similar control mechanisms operate in eukaryotic viruses (e.g. human immunodeficiency virus). A recombinant strain of E. coli
producing relatively large amounts of NusB protein (about 10% of cell protein) was constructed. The protein could be purified with high yield by anion-exchange Chromatography followed by gel-permeation chromatography. The protein is a monomer of 15.6 kDa as shown by analytical ultracentrifugation. Structural studies were performed using protein samples labelled with "N, "C and *H in various combinations.
Heteronuclear three-dimensional triple-resonance NMR experiments combined with a semi-automatic assignment
procedure yielded the sequential assignment of the 'H, "C and "N backbone resonances. Based on experimentally derived scalar couplings, chemical-shift values, amide-exchange data, and a semiquantitative interpretation of NOE data, the secondary structure of NusB has classified as (x helical, comprising
seven a helices.
|Institutions:||Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Prof. Dr. Ruth Gschwind|
|Keywords:||NusB protein; secondary structure ; NMR; antitermination ; N-utilization protein|
|Subjects:||500 Science > 570 Life sciences|
500 Science > 540 Chemistry & allied sciences
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||No|
|Deposited On:||10 Nov 2009 15:45|
|Last Modified:||10 Nov 2009 15:56|