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J. Biol. Chem., Vol. 275, Issue 33, 25069-25072, August 18, 2000

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ACCELERATED PUBLICATION
Stabilization of Circular rpsT mRNA Demonstrates the 5'-End Dependence of RNase E Action in Vivo^*

George A. Mackie

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.

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