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ThemrsC gene ofEscherichia coli is required for mRNA turnover and cell growth, and strains containing the temperature-sensitivemrsC505 allele have longer half-lives than wild-type controls for total pulse-labeled and individual mRNAs (L. L. Granger et al., J. Bacteriol. 180:1920–1928, 1998). The clonedmrsC gene contains a long open reading frame beginning at an initiator UUG codon, confirmed by N-terminal amino acid sequencing, encoding a 70,996-Da protein with a consensus ATP-binding domain.mrsC is identical to the independently identifiedftsH gene except for three additional amino acids at the N terminus (T. Tomoyasu et al., J. Bacteriol. 175:1344–1351, 1993). The purified protein had aKm of 28 μM for ATP and aV max of 21.2 nmol/μg/min. An amino-terminal glutathioneS -transferase–MrsC fusion protein retained ATPase activity but was not biologically active. A glutamic acid replacement of the highly conserved lysine within the ATP-binding motif (mrsC201 ) abolished the complementation of themrsC505 mutation, confirming that the ATPase activity is required for MrsC function in vivo. In addition, themrsC505 allele conferred a temperature-sensitive HflB phenotype, while thehflB29 mutation promoted mRNA stability at both 30 and 44°C, suggesting that the inviability associated with themrsC505 allele is not related to the defect in mRNA decay. The data presented provide the first direct evidence for the involvement of a membrane-bound protein in mRNA decay inE. coli.

Escherichia coli mrsC Is an Allele of hflB , Encoding a Membrane-Associated ATPase and Protease That Is Required for mRNA Decay