An mRNA structure that controls gene expression by binding FMN

Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15908-13. doi: 10.1073/pnas.212628899. Epub 2002 Nov 27.

Abstract

The RFN element is a highly conserved domain that is found frequently in the 5'-untranslated regions of prokaryotic mRNAs that encode for flavin mononucleotide (FMN) biosynthesis and transport proteins. We report that this domain serves as the receptor for a metabolite-dependent riboswitch that directly binds FMN in the absence of proteins. Our results also indicate that in Bacillus subtilis, the riboswitch most likely controls gene expression by causing premature transcription termination of the ribDEAHT operon and precluding access to the ribosome-binding site of ypaA mRNA. Sequence and structural analyses indicate that the RFN element is a natural FMN-binding aptamer, the allosteric character of which is harnessed to control gene expression.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 5' Untranslated Regions / metabolism
  • Allosteric Regulation
  • Bacillus subtilis / genetics*
  • Base Sequence
  • Carrier Proteins / genetics
  • Escherichia coli Proteins / genetics
  • Flavin Mononucleotide / metabolism*
  • Flavin-Adenine Dinucleotide / metabolism
  • Gene Expression Regulation, Bacterial*
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Nucleotide Deaminases / genetics
  • RNA, Bacterial / metabolism*
  • RNA, Messenger / metabolism*
  • Regulatory Sequences, Nucleic Acid*
  • Riboflavin / metabolism
  • Structure-Activity Relationship
  • Sugar Alcohol Dehydrogenases / genetics
  • Transcription, Genetic

Substances

  • 5' Untranslated Regions
  • Carrier Proteins
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • RNA, Bacterial
  • RNA, Messenger
  • riboflavin-binding protein
  • Flavin-Adenine Dinucleotide
  • Flavin Mononucleotide
  • Sugar Alcohol Dehydrogenases
  • RibD protein, E coli
  • Nucleotide Deaminases
  • Riboflavin