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J. Biol. Chem., Vol. 275, Issue 33, 25069-25072, August 18, 2000
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From the Department of Biochemistry and Molecular Biology,
University of British Columbia, Vancouver,
British Columbia V6T 1Z3, Canada
RNase E is the major intracellular endonuclease
in Escherichia coli. Its ability to cleave susceptible
substrates in vitro depends on both the cleavage site
itself and the availability of an unstructured 5' terminus. To test
whether RNase E activity is 5'-end-dependent in
vivo in the presence of all the components of the RNA degradative
machinery, a known substrate, the rpsT mRNA, has been
embedded in a permuted group I intron to permit its efficient, precise
circularization in E. coli. Circular rpsT mRNAs are 4-6-fold more stable in vivo than their
linear counterparts. Even partial inactivation of RNase E activity
further enhances this stability 6-fold. However, the stabilization of
circular rpsT mRNAs depends strongly on their efficient
translation. These results show unambiguously the importance of an
accessible 5'-end in controlling mRNA stability in vivo
and support a two-step ("looping") model for RNase E action in
which the first step is end recognition and the second is actual cleavage.
ACCELERATED PUBLICATION
Stabilization of Circular rpsT mRNA Demonstrates
the 5'-End Dependence of RNase E Action in Vivo*
*
This work was supported by the Medical Research Council of
Canada.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: Dept. of Biochemistry
and Molecular Biology, D. H. Copp Bldg., University of British Columbia, 2146 Health Sciences Mall, Vancouver, B.C. V6T 1Z3, Canada. Tel.: 604-822-2792; Fax: 604-822-5227; E-mail:
gamackie@interchange.ubc.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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