Frameshifting in the expression of the E. coli trpR gene occurs by the bypassing of a segment of its coding sequence

Cell. 1993 Jan 15;72(1):121-30. doi: 10.1016/0092-8674(93)90056-v.

Abstract

The E. coli trpR gene encodes the 108 amino acid long trp repressor. We have previously shown that a +1 frameshifting event occurs during the expression of trpR. Here we show that the transition from the 0 to the +1 frame of trpR occurs by the bypassing of a 55 nt long segment of the trpR+1-lacZ mRNA. This bypassing event is not pretranslational, and it probably takes place during translation. Two adjacent elements are required: a specific sequence of trpR, which must be preceded by a nonspecific 5' end longer than 10 translatable codons. Unique to trpR-lacZ bypassing is that the 55 nt long region must be translated in frame 0 to enable bypassing into the +1 frame. Translational bypassing as a newly discovered mechanism of gene expression is discussed, and the possible existence of translational introns is suggested.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Codon
  • DNA, Bacterial
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Exons
  • Gene Expression Regulation, Bacterial*
  • Genes, Bacterial
  • Introns
  • Lac Operon
  • Molecular Sequence Data
  • Protein Biosynthesis
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism
  • Restriction Mapping
  • Tryptophan / metabolism*

Substances

  • Bacterial Proteins
  • Codon
  • DNA, Bacterial
  • Repressor Proteins
  • TRPR protein, E coli
  • Tryptophan