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Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein

Huenges, M. and Rölz, C. and Gschwind, R. M. and Peteranderl, R. and Berglechner, F. and Richter, G. and Bacher, A. and Kessler, H. and Gemmecker, G. (1998) Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein. The EMBO Journal 17 (14), pp. 4092-4100.

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Abstract

The NusB protein of Escherichia coli is involved in the regulation of rRNA biosynthesis by transcriptional antitermination. In cooperation with several other proteins, it binds to a dodecamer motif designated rrn boxA on the nascent rRNA. The antitermination proteins of E.coli are recruited in the replication cycle of bacteriophage lambda, where they play an important role in switching from the ...

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Item Type:Article
Date:1998
Institutions:Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Prof. Dr. Ruth Gschwind
Identification Number:
ValueType
10.1093/emboj/17.14.4092DOI
Keywords:antitermination; transcription; NusB protein; NMR spectroscopy; RNA-binding protein
Subjects:500 Science > 570 Life sciences
500 Science > 540 Chemistry & allied sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:No
Owner: Nikola Kastner-Pustet
Deposited On:10 Nov 2009 15:56
Last Modified:10 Nov 2009 15:56
Item ID:10658
Owner Only: item control page
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