Increased expression of a eukaryotic gene in Escherichia coli through stabilization of its messenger RNA.

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Abstract
The expression of a cloned eukaryotic gene [catabolic dehydroquinase (3-dehydroquinate hydro-lyase, EC 4.2.1.10) (qa-2+) from Neurospora crassa] is dramatically increased (as much as 100-fold) in E. coli strains deficient in polynucleotide phosphorylase (pnp) (polynucleotide: orthophosphate nucleotidyltransferase, EC 2.7.7.8) and RNase I (rna). The increased expression is controlled primarily by the absence of polynucleotide phosphorylase and appears to be specific for the eukaryotic gene. No increase in the specific activity of either chromosomal or plasmid-borne prokaryotic genes was observed. In polynucleotide phosphorylase-deficient strains of E. coli the half-life of plasmid (pVK88, amp4 qa-2+)-encoded mRNA increases from 1.0 to 2.8 min. This increase must be due primarily to stabilization of the qa-2 mRNA because no increase in the half-lives of pBR322 vehicle mRNA was observed in polynucleotide phosphorylase-deficient strains. There are apparently inherent structural differences between prokaryotic and eukaryotic mRNA.

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