Ribosomes regulate the stability and action of the exoribonuclease RNase R

Wenxing Liang, Murray P Deutscher

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Ribonucleases play an important role in RNA metabolism. Yet, they are also potentially destructive enzymes whose activity must be controlled. Here we describe a novel regulatory mechanism affecting RNase R, a 3' to 5' exoribonuclease able to act on essentially all RNAs including those with extensive secondary structure. Most RNaseRis sequestered on ribosomes in growing cells where it is stable and participates in trans-translation. In contrast, the free form of the enzyme, which is deleterious to cells, is extremely unstable, turning over with a half-life of 2 min. RNaseRbinding to ribosomes is dependent on transfer-messenger RNA (tmRNA)-SmpB, nonstop mRNA, and the modified form of ribosomal protein S12. Degradation of the free form of RNase R also requires tmRNA-SmpB, but this process is independent of ribosomes, indicating two distinct roles for tmRNA-SmpB. Inhibition of RNase R binding to ribosomes leads to slower growth and a massive increase in RNA degradation. These studies indicate a previously unknown role for ribosomes in cellular homeostasis.

Original languageEnglish
Pages (from-to)34791-34798
Number of pages8
JournalJournal of Biological Chemistry
Volume288
Issue number48
DOIs
StatePublished - Nov 29 2013

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Exoribonucleases
Ribosomes
Messenger RNA
Transfer RNA
RNA
Degradation
Enzyme activity
Ribonucleases
Metabolism
RNA Stability
Enzymes
Half-Life
Homeostasis
ribonuclease R
Growth

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Ribosomes regulate the stability and action of the exoribonuclease RNase R. / Liang, Wenxing; Deutscher, Murray P.

In: Journal of Biological Chemistry, Vol. 288, No. 48, 29.11.2013, p. 34791-34798.

Research output: Contribution to journalArticle

Liang, Wenxing ; Deutscher, Murray P. / Ribosomes regulate the stability and action of the exoribonuclease RNase R. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 48. pp. 34791-34798.
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