Acetylation Regulates the Stability of a Bacterial Protein: Growth Stage-Dependent Modification of RNase R

Wenxing Liang, Arun Malhotra, Murray P Deutscher

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

RNase R, an Escherichia coli exoribonuclease important for degradation of structured RNAs, increases 3- to 10-fold under certain stress conditions, due to an increased half-life for this usually unstable protein. Components of the trans-translation machinery, tmRNA, and its associated protein, SmpB, are essential for RNase R instability. However, it is not understood why exponential phase RNase R is unstable or how it becomes stabilized in stationary phase. Here, we show that these phenomena are regulated by acetylation catalyzed by YfiQ protein. One residue, Lys544, is acetylated in exponential phase RNase R, but not in the stationary phase protein, resulting in tighter binding of tmRNA-SmpB to the C-terminal region of exponential phase RNase R and subsequent proteolytic degradation. Removal of the positive charge at Lys544 or a negative charge in the C-terminal region likely disrupts their interaction, facilitating tmRNA-SmpB binding. These findings indicate that acetylation can regulate the stability of a bacterial protein.

Original languageEnglish
Pages (from-to)160-166
Number of pages7
JournalMolecular Cell
Volume44
Issue number1
DOIs
StatePublished - Oct 7 2011

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Bacterial Proteins
Acetylation
Growth
Exoribonucleases
Proteins
RNA Stability
Half-Life
ribonuclease R
Escherichia coli
tmRNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Acetylation Regulates the Stability of a Bacterial Protein : Growth Stage-Dependent Modification of RNase R. / Liang, Wenxing; Malhotra, Arun; Deutscher, Murray P.

In: Molecular Cell, Vol. 44, No. 1, 07.10.2011, p. 160-166.

Research output: Contribution to journalArticle

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