PMID:22124017
| Citation |
Liang, W and Deutscher, MP (2012) Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ). RNA 18:37-41 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC3261742 Online version:10.1261/rna.030213.111 |
| Keywords |
Acetyltransferases/metabolism; Enzyme Stability; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins/metabolism; Exoribonucleases/genetics; Exoribonucleases/metabolism; Protein Processing, Post-Translational; RNA, Bacterial/metabolism; Stress, Physiological |
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