NusG overexpression inhibits Rho-dependent termination in Escherichia coli.
The Escherichia coli NusG protein binds Rho in vitro and is required for efficient Rho-dependent transcription termination in vivo. In this work we examine transcription termination in cells that over-express NusG. Termination at the Rho-dependent lambda tL1 and lambda tR1 sites was significantly inhibited by excess NusG, whereas the Rho-independent lambda tl site was fully functional. Although Western analysis showed no reduction in the levels of soluble Rho, termination was restored when Rho was also overexpressed. Our data indicated that the ratio of NusG and Rho proteins affects the efficiency of transcription termination.
Burova
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Institute of Cancer Research, College of Physicians and Surgeons of Columbia University, New York, New York 10032, USA.
Gottesman
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D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D015151:Immunoblotting; D008957:Models, Genetic; D010445:Peptide Elongation Factors / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D012234:Rho Factor / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic; D001616:beta-Galactosidase / Q000096:biosynthesis
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C070291:NusG protein, E coli; D010445:Peptide Elongation Factors; D011994:Recombinant Proteins; D012234:Rho Factor; D014157:Transcription Factors; D001616:beta-Galactosidase