Effects of FIS Protein on rnpB Transcription in Escherichia coli

  • Choi, Hyun-Sook (Department of Chemistry and Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology) ;
  • Kim, Kwang-sun (Department of Chemistry and Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology) ;
  • Park, Jeong Won (Department of Chemistry and Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology) ;
  • Jung, Young Hwan (Department of Chemistry and Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology) ;
  • Lee, Younghoon (Department of Chemistry and Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology)
  • Received : 2004.11.09
  • Accepted : 2004.12.16
  • Published : 2005.04.30

Abstract

Factor for inversion stimulation (FIS), the Escherichia coli protein, is a positive regulator of the transcription of genes that encode stable RNA species, such as rRNA and tRNA. Transcription of the rnpB gene encoding M1 RNA, the catalytic subunit of E. coli RNase P, rapidly declines under stringent conditions, as does that of other stable RNAs. There are multiple putative FIS binding sites upstream of the rnpB promoter. We tested whether FIS binds to these sites, and if so, how it affects rnpB transcription. In vitro binding assays revealed specific binding of FIS to multiple sites in the rnpB promoter region. Interestingly, FIS bound not only to the upstream region of the promoter, but also to the region from +4 to +18. FIS activated rnpB transcription in vitro, but the level of activation was much lower than that of the rrnB promoter for rRNA. We also examined the effects of FIS on rnpB transcription in vivo using isogenic $fis^+$ and $fis^-$ strains. rnpB transcription was higher in the $fis^-$ than the $fis^+$ cells during the transitions from lag to exponential phase, and from exponential to stationary phase.

Keywords

Acknowledgement

Supported by : Korea Research Foundation

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