Two Structurally Independent Domains of E. coli NusG Create Regulatory Plasticity via Distinct Interactions with RNA Polymerase and Regulators

Titelangaben

Mooney, Rachel A. ; Schweimer, Kristian ; Rösch, Paul ; Gottesman, Max E. ; Landick, Robert:
Two Structurally Independent Domains of E. coli NusG Create Regulatory Plasticity via Distinct Interactions with RNA Polymerase and Regulators.
In: Journal of Molecular Biology. Bd. 391 (2009) Heft 2 . - S. 341-358.
ISSN 0022-2836
DOI: https://doi.org/10.1016/j.jmb.2009.05.078

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Abstract

NusG is a conserved regulatory protein that interacts with elongation complexes (ECs) of RNA polymerase, DNA, and RNA to modulate transcription in multiple and sometimes opposite ways. In Escherichia coli, NusG suppresses pausing and increases elongation rate, enhances termination by E. coli ρ and phage HK022 Nun protein, and promotes antitermination by λN and in ribosomal RNA operons. We report NMR studies that suggest that E. coli NusG consists of two largely independent N-and C-terminal structural domains