RNase R is a processive exoribonuclease that plays an important role in degradation of structured RNAs in Escherichia coli. RNase R is unstable in exponential phase cells; however, under certain stress conditions, RNase R levels increase dramatically due to its stabilization. Binding of tmRNA and SmpB to the C-terminal region of RNase R is required for its instability, and this binding is regulated by acetylation of a single residue, Lys544, in exponential phase cells. RNase R is not acetylated in stationary phase. We show here that only exponential phase RNase R is acetylated because the modifying enzyme, protein lysine acetyltransferase, Pka (YfiQ), is absent from late exponential and stationary phase cells. As a consequence, newly synthesized RNase R remains unmodified. Together with the turnover of preexisting acetylated RNase R, no modified RNase R remains in stationary phase. We find that RNase R in cold-shocked cells also lacks the acetyl modification due to the absence of Pka. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions.
- Escherichia coli
- Post-translational modification
- Protein stability
ASJC Scopus subject areas
- Molecular Biology