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Vol. 12, No. 5, pp. 745-754, March 1, 1998

RESEARCH PAPER
Conversion of the omega  subunit of Escherichia coli RNA polymerase into a transcriptional activator or an activation target

Simon L. Dove, and Ann Hochschild1

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115 USA

Evidence obtained in both eukaryotes and prokaryotes indicates that arbitrary contacts between DNA-bound proteins and components of the transcriptional machinery can activate transcription. Here we demonstrate that the Escherichia coli omega  protein, which copurifies with RNA polymerase, can function as a transcriptional activator when linked covalently to a DNA-binding protein. We show further that omega  can function as an activation target when this covalent linkage is replaced by a pair of interacting polypeptides fused to the DNA-binding protein and to omega , respectively. Our findings imply that the omega  protein is associated with RNA polymerase holoenzyme in vivo, and provide support for the hypothesis that contact between a DNA-bound protein and any component of E. coli RNA polymerase can activate transcription.

[Key Words: theta subunit; E. coli; RNA polymerase; transcriptional activator]


GENES & DEVELOPMENT 12:745-754 © 1998 by Cold Spring Harbor Laboratory Press  ISSN 0890-9369/98 $5.00

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