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Nucleic Acids Research, 1994, Vol. 22, No. 3 397-403
© 1994

MOLECULAR BIOLOGY

Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation

Murielle Robert-Le Meur and Claude Portier*

Institut de Biologie Physico-Chimique CNRS (URA119), 13 rue Pierre et Marie Curie, 75005 Paris, France

* To whom correspondence should be addressed

Received September 23, 1993. Accepted December 20, 1993.

Polynucleotlde phosphorylase, a 3' to 5' processive exorlbonuclease Is post-transcriptionally autocon-trolled and it was previously shown that this control is dependent on a 5' processing by RNase III. In this paper, the mechanism of regulation is analyzed by studying the properties of a pnp-iacZ translational gene fusion. It is shown that this message is stable, even when processed by RNase III, and that the degradation rate is directly linked to the intracellular concentration of polynucleotlde phosphorylase or to the pnp-lacZ messenger translation rate. Mutations able to decrease the level of repression are all located in the ribosome loading site. Taken together, these results suggest that polynucleotide phosphorylase Is able to recognize specifically the processed messenger and to prevent Its translation, thus allowing degradation of the message.


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