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AdivE mutant, which has a temperature-sensitive mutation in the tRNA1 Ser gene, exhibits differential loss of the synthesis of certain proteins, such as β-galactosidase and succinate dehydrogenase, at nonpermissive temperatures. InEscherichia coli , the UCA codon is recognized only by tRNA1 Ser . Several genes containing UCA codons are normally expressed after a temperature shift to 42°C in thedivE mutant. Therefore, it is unlikely that the defect in protein synthesis at 42°C is simply caused by a defect in the decoding function of the mutant tRNA1 Ser . In this study, we sought to determine the cause of the defect inlacZ gene expression in thedivE mutant. It has also been shown that the defect inlacZ gene expression is accompanied by a decrease in the amount oflacZ mRNA. To examine whether inactivation of mRNA degradation pathways restores the defect inlacZ gene expression, we constructeddivE mutants containingrne-1 ,rnb-500 , andpnp-7 mutations in various combinations. We found that the defect was almost completely restored by introducing anrne-1 pnp-7 double mutation into thedivE mutant. Northern hybridization analysis showed that therne-1 mutation stabilizedlacZ mRNA, whereas thepnp-7 mutation stabilized mutant tRNA1 Ser , at 44°C. We present a mechanism that may explain these results.

An rne-1 pnp-7 Double Mutation Suppresses the Temperature-Sensitive Defect of lacZ Gene Expression in a divE Mutant