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J. Biol. Chem., Vol. 277, Issue 19, 17095-17100, May 10, 2002
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From the Department of Biological Sciences, Stanford University,
Stanford, California 94305-5020
Expression of the tryptophanase (tna)
operon in Escherichia coli is regulated by catabolite
repression and tryptophan-induced transcription antitermination.
The key feature of this antitermination mechanism has been shown to be
the retention of uncleaved TnaC-peptidyl-tRNA in the translating
ribosome. This ribosome remains stalled at the tna stop
codon and blocks the access of Rho factor to the tna
transcript, thereby preventing transcription termination. In normal
S-30 preparations, synthesis of a TnaC peptide containing arginine
instead of tryptophan at position 12 (Arg12-TnaC) was shown
to be insensitive to added tryptophan, i.e.
Arg12-TnaC-peptidyl-tRNA was cleaved, and there was normal
Rho-dependent transcription termination. When the S-30
extract used was depleted of release factor 2, Arg12-TnaC-tRNAPro was accumulated in the
absence or presence of added tryptophan. Under these conditions the
accumulation of Arg12-TnaC-tRNAPro prevented
Rho-dependent transcription termination, mimicking normal
induction. Using a minimal in vitro transcription system consisting of a tna template, RNA polymerase, and Rho, it
was shown that RNA sequences immediately adjacent to the
tnaC stop codon, the presumed boxA and
rut sites, contributed most significantly to
Rho-dependent termination. The tna boxA-like
sequence appeared to serve as a segment of the Rho "entry" site,
despite its likeness to the boxA element.
Analysis of Tryptophanase Operon Expression in Vitro
ACCUMULATION OF TnaC-PEPTIDYL-tRNA IN A RELEASE FACTOR
2-DEPLETED S-30 EXTRACT PREVENTS Rho FACTOR ACTION, SIMULATING
INDUCTION*
*
This work was supported by Grant MCB-0093023 from the
National Science Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel: 650-725-1835;
Fax: 650-725-8221; E-mail: yanofsky@cmgm.stanford.edu.
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