and
George Georgiou1,3,4*
Institute for Cell and Molecular Biology, University of Texas at Austin, Austin, Texas 78712,1 Graduate Program in Microbiology, University of Texas at Austin, Austin, Texas 78712,2 Department of Chemical Engineering, University of Texas at Austin, Austin, Texas 78712,3 Department of Biomedical Engineering, University of Texas at Austin, Austin, Texas 787124
Received 18 November 2005/ Accepted 21 February 2006
The recently discovered RraA protein acts as an inhibitor of the essential endoribonuclease RNase E, and we demonstrated that ectopic expression of RraA affects the abundance of more than 700 transcripts in Escherichia coli (K. Lee, X. Zhan, J. Gao, J. Qiu, Y. Feng, R. Meganathan, S. N. Cohen, and G. Georgiou, Cell 114:623-634, 2003). We show that rraA is expressed from its own promoter, PrraA, located in the menA-rraA intergenic region. Primer extension and lacZ fusion analysis revealed that transcription from PrraA is elevated upon entry into stationary phase in a
s-dependent manner. In addition, the stability of the rraA transcript is dependent on RNase E activity, suggesting the involvement of a feedback circuit in the regulation of the RraA level in E. coli.
Present address: Graduate School of Bio and Agricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
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