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J Biol Chem, Vol. 273, Issue 32, 20494-20503, August 7, 1998
From the Department of Biochemistry and Molecular Biology,
Pennsylvania State University,
University Park, Pennsylvania 16802
Expression of the trpEDCFBA operon is
regulated at both the transcriptional and translational levels by the
trp RNA-binding attenuation protein (TRAP) of
Bacillus subtilis. When cells contain sufficient levels of
tryptophan to activate TRAP, the protein binds to trp
operon transcripts as they are being synthesized, most often causing
transcription termination. However, termination is never 100%
efficient, and transcripts that escape termination are subject to
translational control. We determined that TRAP-mediated translational
control of trpE can occur via a novel RNA conformational switch mechanism. When TRAP binds to the 5'-untranslated leader segment
of a trp operon read-through transcript, it can disrupt a
large secondary structure containing a portion of the TRAP binding target. This promotes refolding of the RNA such that the
trpE Shine-Dalgarno sequence, located more than 100 nucleotides downstream from the TRAP binding site, becomes sequestered
in a stable RNA hairpin. Results from cell-free translation, ribosome
toeprint, and RNA structure mapping experiments demonstrate that
formation of this structure reduces TrpE synthesis by blocking ribosome access to the trpE ribosome binding site. The role of the
Shine-Dalgarno blocking hairpin in controlling translation of
trpE was confirmed by examining the effect of multiple
nucleotide substitutions that abolish the structure without altering
the Shine-Dalgarno sequence itself. The possibility of protein-mediated
RNA refolding as a general mechanism in controlling gene expression is
discussed.
trp RNA-binding Attenuation Protein-mediated Long
Distance RNA Refolding Regulates Translation of trpE in
Bacillus subtilis
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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